UniProtKB - O33194 (G3PP_MYCTU)
Protein
D,L-glycerol 3-phosphate phosphatase
Gene
Rv1692
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
Glycerol-phosphate phosphatase with a preference for D-glycerol 3-phosphate (sn-glycerol 1-phosphate) over L-glycerol 3-phosphate (sn-glycerol 3-phosphate). Is the final enzyme involved in the recycling/catabolism of glycerophospholipid polar heads. To a lesser extent, is also able to act on glycerol 2-phosphate and D-ribulose 5-phosphate, but cannot use D-glyceraldehyde 3-phosphate, dihydroxyacetone-phosphate, UMP or GMP as substrates.1 Publication
Catalytic activityi
- EC:3.1.3.211 Publication
Cofactori
Mg2+1 Publication, Co2+1 Publication, Mn2+1 PublicationNote: Although Co2+ and Mn2+ support eight- and fourfold higher catalytic efficiency than Mg2+, respectively, Mg2+ is likely the physiologically relevant catalytic divalent metal ion.1 Publication
Kineticsi
kcat is 0.77 sec(-1) with D,L-glycerol 3-phosphate as substrate. kcat is 0.18 sec(-1) with D-ribulose 5-phosphate as substrate. kcat is 0.18 sec(-1) with glycerol 2-phosphate as substrate. kcat is 1.00 sec(-1) with p-nitrophenyl 3-phosphate as substrate. kcat is 0.02 sec(-1) with L-glycerol 3-phosphate as substrate.1 Publication
- KM=0.89 mM for D,L-glycerol 3-phosphate1 Publication
- KM=1.30 mM for D-ribulose 5-phosphate1 Publication
- KM=2.01 mM for glycerol 2-phosphate1 Publication
- KM=19.30 mM for p-nitrophenyl 3-phosphate1 Publication
- KM=1.10 mM for L-glycerol 3-phosphate1 Publication
: Glycerolipid metabolism Pathwayi
This protein is involved in Glycerolipid metabolism.1 PublicationView all proteins of this organism that are known to be involved in Glycerolipid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 14 | NucleophileBy similarity | 1 | |
Metal bindingi | 14 | MagnesiumCombined sources1 Publication | 1 | |
Active sitei | 16 | Proton donorBy similarity | 1 | |
Metal bindingi | 16 | Magnesium; via carbonyl oxygenCombined sources1 Publication | 1 | |
Metal bindingi | 209 | MagnesiumCombined sources1 Publication | 1 |
GO - Molecular functioni
- cobalt ion binding Source: UniProtKB
- glycerol-1-phosphatase activity Source: UniProtKB
- magnesium ion binding Source: UniProtKB
- manganese ion binding Source: UniProtKB
- phosphatase activity Source: GO_Central
- protein homodimerization activity Source: UniProtKB
GO - Biological processi
- glycerol metabolic process Source: UniProtKB-KW
- glycerophospholipid catabolic process Source: UniProtKB
Keywordsi
Molecular function | Hydrolase |
Biological process | Glycerol metabolism |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyci | MTBH37RV:G185E-5883-MONOMER |
Chemistry databases
SwissLipidsi | SLP:000001039 |
Names & Taxonomyi
Protein namesi | Recommended name: D,L-glycerol 3-phosphate phosphatase1 Publication (EC:3.1.3.211 Publication)Short name: G3P phosphatase1 Publication |
Gene namesi | Ordered Locus Names:Rv1692Imported, LH57_09220Imported |
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 | Rv1692 |
Pathology & Biotechi
Disruption phenotypei
Deletion of this gene results in an accumulation of G3P and G3P-containing lipid polar heads.1 Publication
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000435901 | 1 – 353 | D,L-glycerol 3-phosphate phosphataseAdd BLAST | 353 |
Proteomic databases
PaxDbi | O33194 |
PRIDEi | O33194 |
Interactioni
Subunit structurei
Homodimer.
1 PublicationGO - Molecular functioni
- protein homodimerization activity Source: UniProtKB
Protein-protein interaction databases
STRINGi | 83332.Rv1692 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | O33194 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domaini
Crystal structures of Rv1692 reveal a unique architecture, a fusion of a predicted haloacid dehalogenase fold with a previously unidentified GCN5-related N-acetyltransferase (GNAT) region. Although not directly involved in acetyl transfer, or regulation of enzymatic activity in vitro, the GNAT region is critical for the solubility of the phosphatase.1 Publication
Sequence similaritiesi
Belongs to the HAD-like hydrolase superfamily.Curated
Phylogenomic databases
eggNOGi | ENOG4105DSU Bacteria COG0647 LUCA |
HOGENOMi | HOG000068103 |
KOi | K06117 |
OMAi | PPMHRET |
PhylomeDBi | O33194 |
Family and domain databases
Gene3Di | 3.40.50.1000, 2 hits |
InterProi | View protein in InterPro IPR041065 GNAT-like IPR036412 HAD-like_sf IPR006357 HAD-SF_hydro_IIA IPR023214 HAD_sf |
Pfami | View protein in Pfam PF18407 GNAT_like, 1 hit PF13344 Hydrolase_6, 1 hit |
PIRSFi | PIRSF000915 PGP-type_phosphatase, 1 hit |
SUPFAMi | SSF56784 SSF56784, 1 hit |
TIGRFAMsi | TIGR01460 HAD-SF-IIA, 1 hit |
i Sequence
Sequence statusi: Complete.
O33194-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKSIAQEHDC LLIDLDGTVF CGRQPTGGAV QSLSQVRSRK LFVTNNASRS
60 70 80 90 100
ADEVAAHLCE LGFTATGEDV VTSAQSAAHL LAGQLAPGAR VLIVGTEALA
110 120 130 140 150
NEVAAVGLRP VRRFEDRPDA VVQGLSMTTG WSDLAEAALA IRAGALWVAA
160 170 180 190 200
NVDPTLPTER GLLPGNGSMV AALRTATGMD PRVAGKPAPA LMTEAVARGD
210 220 230 240 250
FRAALVVGDR LDTDIEGANA AGLPSLMVLT GVNSAWDAVY AEPVRRPTYI
260 270 280 290 300
GHDLRSLHQD SKLLAVAPQP GWQIDVGGGA VTVCANGDVD DLEFIDDGLS
310 320 330 340 350
IVRAVASAVW EARAADLHQR PLRIEAGDER ARAALQRWSL MRSDHPVTSV
GTQ
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP44457.1 CP009480 Genomic DNA Translation: AIR14443.1 |
RefSeqi | NP_216208.1, NC_000962.3 WP_003408380.1, NZ_NVQJ01000010.1 |
Genome annotation databases
EnsemblBacteriai | AIR14443; AIR14443; LH57_09220 CCP44457; CCP44457; Rv1692 |
GeneIDi | 885241 |
KEGGi | mtu:Rv1692 mtv:RVBD_1692 |
PATRICi | fig|83332.111.peg.1880 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP44457.1 CP009480 Genomic DNA Translation: AIR14443.1 |
RefSeqi | NP_216208.1, NC_000962.3 WP_003408380.1, NZ_NVQJ01000010.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4I9G | X-ray | 3.25 | A/B | 1-353 | [»] | |
SMRi | O33194 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv1692 |
Chemistry databases
SwissLipidsi | SLP:000001039 |
Proteomic databases
PaxDbi | O33194 |
PRIDEi | O33194 |
Genome annotation databases
EnsemblBacteriai | AIR14443; AIR14443; LH57_09220 CCP44457; CCP44457; Rv1692 |
GeneIDi | 885241 |
KEGGi | mtu:Rv1692 mtv:RVBD_1692 |
PATRICi | fig|83332.111.peg.1880 |
Organism-specific databases
TubercuListi | Rv1692 |
Phylogenomic databases
eggNOGi | ENOG4105DSU Bacteria COG0647 LUCA |
HOGENOMi | HOG000068103 |
KOi | K06117 |
OMAi | PPMHRET |
PhylomeDBi | O33194 |
Enzyme and pathway databases
BioCyci | MTBH37RV:G185E-5883-MONOMER |
Family and domain databases
Gene3Di | 3.40.50.1000, 2 hits |
InterProi | View protein in InterPro IPR041065 GNAT-like IPR036412 HAD-like_sf IPR006357 HAD-SF_hydro_IIA IPR023214 HAD_sf |
Pfami | View protein in Pfam PF18407 GNAT_like, 1 hit PF13344 Hydrolase_6, 1 hit |
PIRSFi | PIRSF000915 PGP-type_phosphatase, 1 hit |
SUPFAMi | SSF56784 SSF56784, 1 hit |
TIGRFAMsi | TIGR01460 HAD-SF-IIA, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | G3PP_MYCTU | |
Accessioni | O33194Primary (citable) accession number: O33194 Secondary accession number(s): F2GK45, I6XYN9, Q7D849 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 13, 2016 |
Last sequence update: | January 1, 1998 | |
Last modified: | October 16, 2019 | |
This is version 130 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, 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