UniProtKB - P9WQB1 (DHA_MYCTU)
Protein
Alanine dehydrogenase
Gene
ald
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
Catalyzes the reversible reductive amination of pyruvate to L-alanine. However, since the physiological environment of M.tuberculosis has a neutral pH, it can be assumed that the enzyme catalyzes exclusively the formation of L-alanine. May play a role in cell wall synthesis as L-alanine is an important constituent of the peptidoglycan layer.1 Publication
Miscellaneous
L-alanine dehydrogenase activity increases when the M.tuberculosis is shifted from aerobic to anaerobic growth conditions.1 Publication
Catalytic activityi
- EC:1.4.1.12 Publications
Cofactori
Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication
Activity regulationi
Inhibited by CuSO4 and ZnCl2.1 Publication
Kineticsi
- KM=98.2 µM for NADH (at pH 7.4 and at 37 degrees Celsius)1 Publication
- KM=0.31 mM for NAD (at pH 10.2 and at 37 degrees Celsius)1 Publication
- KM=0.76 mM for pyruvate (at pH 7.4 and at 25 degrees Celsius)1 Publication
- KM=1.45 mM for pyruvate (at pH 7.4 and at 37 degrees Celsius)1 Publication
- KM=13.8 mM for L-alanine (at pH 10.2 and at 37 degrees Celsius)1 Publication
- KM=15.6 mM for L-alanine (at pH 10.2 and at 25 degrees Celsius)1 Publication
- KM=35.4 mM for ammonium (at pH 7.4 and at 37 degrees Celsius)1 Publication
- Vmax=31.8 µmol/min/mg enzyme for reductive amination1 Publication
- Vmax=23.7 µmol/min/mg enzyme for oxidative deamination1 Publication
pH dependencei
Optimum pH is between 10 and 11 for the oxidative deamination and between 7 and 7.5 for the reductive amination.1 Publication
Temperature dependencei
Relatively stable, it loses only 25% of its total activity after 4 hours at 60 degrees Celsius. The enzyme is much more active at temperatures above 37 degrees Celsius, particularly in the reductive amination. The velocity almost doubles at temperatures between 60-65 degrees Celsius compared with 37 degrees Celsius. Above 65 degrees Celsius there is a sharp decrease in activity, due to thermal inactivation of the enzyme.2 Publications
: L-alanine degradation via dehydrogenase pathway Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes NH(3) and pyruvate from L-alanine.Proteins known to be involved in this subpathway in this organism are:
- Alanine dehydrogenase (ald)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes NH(3) and pyruvate from L-alanine, the pathway L-alanine degradation via dehydrogenase pathway and in Amino-acid degradation.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 15 | Substrate1 Publication | 1 | |
Binding sitei | 75 | Substrate1 Publication | 1 | |
Active sitei | 96 | Proton donor/acceptor1 Publication | 1 | |
Binding sitei | 134 | NAD2 Publications | 1 | |
Binding sitei | 198 | NAD2 Publications | 1 | |
Binding sitei | 203 | NAD2 Publications | 1 | |
Binding sitei | 220 | NAD2 Publications | 1 | |
Active sitei | 270 | Proton donor/acceptor1 Publication | 1 | |
Binding sitei | 279 | NAD2 Publications | 1 | |
Metal bindingi | 323 | MagnesiumCombined sources1 Publication | 1 | |
Metal bindingi | 327 | Magnesium; via tele nitrogenCombined sources1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 178 – 179 | NAD2 Publications | 2 | |
Nucleotide bindingi | 239 – 240 | NAD2 Publications | 2 | |
Nucleotide bindingi | 267 – 270 | NAD2 Publications | 4 | |
Nucleotide bindingi | 298 – 301 | NAD2 Publications | 4 |
GO - Molecular functioni
- alanine dehydrogenase activity Source: MTBBASE
- metal ion binding Source: UniProtKB-KW
- nucleotide binding Source: UniProtKB-KW
GO - Biological processi
- alanine catabolic process Source: MTBBASE
- L-alanine catabolic process Source: UniProtKB-UniPathway
- response to hypoxia Source: MTBBASE
Keywordsi
Molecular function | Oxidoreductase |
Ligand | Magnesium, Metal-binding, NAD, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | MTBH37RV:G185E-7029-MONOMER |
UniPathwayi | UPA00527;UER00585 |
Names & Taxonomyi
Protein namesi | Recommended name: Alanine dehydrogenase (EC:1.4.1.12 Publications)Alternative name(s): 40 kDa antigen TB43 |
Gene namesi | Name:ald Ordered Locus Names:Rv2780 ORF Names:MTV002.45 |
Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic identifieri | 83332 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
Organism-specific databases
TubercuListi | Rv2780 |
Subcellular locationi
- Secreted 1 Publication
GO - Cellular componenti
- cell wall Source: MTBBASE
- cytosol Source: MTBBASE
- extracellular region Source: MTBBASE
- plasma membrane Source: MTBBASE
Keywords - Cellular componenti
SecretedPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 96 | H → A: Completely inactive mutant. 1 Publication | 1 | |
Mutagenesisi | 270 | D → A: Completely inactive mutant. 1 Publication | 1 | |
Mutagenesisi | 270 | D → N: Completely inactive mutant. The bifurcated hydrogen bond between D-270 and the ribose of NAD is replaced by a single hydrogen bond. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000198994 | 1 – 371 | Alanine dehydrogenaseAdd BLAST | 371 |
Proteomic databases
PaxDbi | P9WQB1 |
Expressioni
Inductioni
Upon nutrient starvation.1 Publication
Interactioni
Subunit structurei
Homohexamer. Trimer of dimers.
2 PublicationsProtein-protein interaction databases
STRINGi | 83332.Rv2780 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P9WQB1 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Belongs to the AlaDH/PNT family.Curated
Phylogenomic databases
eggNOGi | ENOG4105DCF Bacteria COG0686 LUCA |
KOi | K00259 |
OMAi | CFETSKA |
PhylomeDBi | P9WQB1 |
Family and domain databases
CDDi | cd05305 L-AlaDH, 1 hit |
InterProi | View protein in InterPro IPR008141 Ala_DH IPR008143 Ala_DH/PNT_CS2 IPR008142 AlaDH/PNT_CS1 IPR007886 AlaDH/PNT_N IPR007698 AlaDH/PNT_NAD(H)-bd IPR036291 NAD(P)-bd_dom_sf |
PANTHERi | PTHR42795 PTHR42795, 1 hit |
Pfami | View protein in Pfam PF01262 AlaDh_PNT_C, 1 hit PF05222 AlaDh_PNT_N, 1 hit |
PIRSFi | PIRSF000183 Alanine_dh, 1 hit |
SMARTi | View protein in SMART SM01002 AlaDh_PNT_C, 1 hit SM01003 AlaDh_PNT_N, 1 hit |
SUPFAMi | SSF51735 SSF51735, 1 hit |
TIGRFAMsi | TIGR00518 alaDH, 1 hit |
PROSITEi | View protein in PROSITE PS00836 ALADH_PNT_1, 1 hit PS00837 ALADH_PNT_2, 1 hit |
i Sequence
Sequence statusi: Complete.
P9WQB1-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MRVGIPTETK NNEFRVAITP AGVAELTRRG HEVLIQAGAG EGSAITDADF
60 70 80 90 100
KAAGAQLVGT ADQVWADADL LLKVKEPIAA EYGRLRHGQI LFTFLHLAAS
110 120 130 140 150
RACTDALLDS GTTSIAYETV QTADGALPLL APMSEVAGRL AAQVGAYHLM
160 170 180 190 200
RTQGGRGVLM GGVPGVEPAD VVVIGAGTAG YNAARIANGM GATVTVLDIN
210 220 230 240 250
IDKLRQLDAE FCGRIHTRYS SAYELEGAVK RADLVIGAVL VPGAKAPKLV
260 270 280 290 300
SNSLVAHMKP GAVLVDIAID QGGCFEGSRP TTYDHPTFAV HDTLFYCVAN
310 320 330 340 350
MPASVPKTST YALTNATMPY VLELADHGWR AACRSNPALA KGLSTHEGAL
360 370
LSERVATDLG VPFTEPASVL A
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 13 | E → EFQ in CAA44791 (PubMed:1587598).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X63069 Genomic DNA Translation: CAA44791.1 U92472 Genomic DNA Translation: AAC38804.1 AL123456 Genomic DNA Translation: CCP45579.1 |
PIRi | C70883 A43830 |
RefSeqi | NP_217296.1, NC_000962.3 WP_003899477.1, NZ_NVQJ01000020.1 |
Genome annotation databases
EnsemblBacteriai | CCP45579; CCP45579; Rv2780 |
GeneIDi | 888493 |
KEGGi | mtu:Rv2780 mtv:RVBD_2780 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X63069 Genomic DNA Translation: CAA44791.1 U92472 Genomic DNA Translation: AAC38804.1 AL123456 Genomic DNA Translation: CCP45579.1 |
PIRi | C70883 A43830 |
RefSeqi | NP_217296.1, NC_000962.3 WP_003899477.1, NZ_NVQJ01000020.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2VHV | X-ray | 2.80 | A/B | 1-371 | [»] | |
2VHW | X-ray | 2.00 | A/B/C/D/E/F | 1-371 | [»] | |
2VHX | X-ray | 2.00 | A/B/C/D/E/F | 1-371 | [»] | |
2VHY | X-ray | 2.30 | A/B | 1-371 | [»] | |
2VHZ | X-ray | 2.04 | A/B | 1-371 | [»] | |
2VOE | X-ray | 2.60 | A/B/C/D/E/F | 1-371 | [»] | |
2VOJ | X-ray | 2.60 | A/C/E | 1-371 | [»] | |
SMRi | P9WQB1 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv2780 |
Proteomic databases
PaxDbi | P9WQB1 |
Genome annotation databases
EnsemblBacteriai | CCP45579; CCP45579; Rv2780 |
GeneIDi | 888493 |
KEGGi | mtu:Rv2780 mtv:RVBD_2780 |
Organism-specific databases
TubercuListi | Rv2780 |
Phylogenomic databases
eggNOGi | ENOG4105DCF Bacteria COG0686 LUCA |
KOi | K00259 |
OMAi | CFETSKA |
PhylomeDBi | P9WQB1 |
Enzyme and pathway databases
UniPathwayi | UPA00527;UER00585 |
BioCyci | MTBH37RV:G185E-7029-MONOMER |
Family and domain databases
CDDi | cd05305 L-AlaDH, 1 hit |
InterProi | View protein in InterPro IPR008141 Ala_DH IPR008143 Ala_DH/PNT_CS2 IPR008142 AlaDH/PNT_CS1 IPR007886 AlaDH/PNT_N IPR007698 AlaDH/PNT_NAD(H)-bd IPR036291 NAD(P)-bd_dom_sf |
PANTHERi | PTHR42795 PTHR42795, 1 hit |
Pfami | View protein in Pfam PF01262 AlaDh_PNT_C, 1 hit PF05222 AlaDh_PNT_N, 1 hit |
PIRSFi | PIRSF000183 Alanine_dh, 1 hit |
SMARTi | View protein in SMART SM01002 AlaDh_PNT_C, 1 hit SM01003 AlaDh_PNT_N, 1 hit |
SUPFAMi | SSF51735 SSF51735, 1 hit |
TIGRFAMsi | TIGR00518 alaDH, 1 hit |
PROSITEi | View protein in PROSITE PS00836 ALADH_PNT_1, 1 hit PS00837 ALADH_PNT_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | DHA_MYCTU | |
Accessioni | P9WQB1Primary (citable) accession number: P9WQB1 Secondary accession number(s): L0TC82, O33322, P30234 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | September 18, 2019 | |
This is version 32 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references