UniProtKB - P9WJA1 (HSAA_MYCTU)
Protein
Flavin-dependent monooxygenase, oxygenase subunit HsaA
Gene
hsaA
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
Catalyzes the o-hydroxylation of 3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione (3-HSA) to 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione (3,4-DHSA) in the catabolism of cholesterol. Can also use 3,17-dihydroxy-9,10-seconandrost-1,3,5(10)-triene-9-one (3,17-DHSA), but it has higher specificity for 3-HSA than for 3,17-DHSA. Can use either FADH2 or FMNH2 as flavin cosubstrate. Also catalyzes the o-hydroxylation of a range of p-substituted phenols to generate the corresponding catechols.1 Publication
Miscellaneous
Cholesterol metabolism contributes to the survival of M.tuberculosis in the host by helping the bacterial multiplication during earlier stages of infection and to the dissemination of the pathogen in the host.
Catalytic activityi
- 3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione + FMNH2 + O2 = 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione + FMN + H+ + H2O1 PublicationEC:1.14.14.121 PublicationThis reaction proceeds in the forward1 Publication direction.
- 3,17-dihydroxy-9,10-secoandrost-1,3,5(10)-triene-9-one + FMNH2 + O2 = 3,4,17-trihydroxy-9,10-secoandrost-1,3,5(10)-triene-9-one + FMN + H+ + H2O1 PublicationThis reaction proceeds in the forward1 Publication direction.
Kineticsi
- KM=97 µM for 3-HSA (with FAD at pH 7 and at 25 degrees Celsius)1 Publication
- KM=100 µM for oxygene (with FMN at pH 7 and at 25 degrees Celsius)1 Publication
- KM=200 µM for 3-HSA (with FMN at pH 7 and at 25 degrees Celsius)1 Publication
- KM=350 µM for 3,17-DHSA (with FMN at pH 7 and at 25 degrees Celsius)1 Publication
- KM=1440 µM for 3-hydroxybiphenyl (3-HB) (with FMN at pH 7 and at 25 degrees Celsius)1 Publication
: steroid biosynthesis Pathwayi
This protein is involved in the pathway steroid biosynthesis, which is part of Lipid metabolism.View all proteins of this organism that are known to be involved in the pathway steroid biosynthesis and in Lipid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 84 | FMNBy similarity | 1 | |
Binding sitei | 263 | FMNBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 118 – 120 | FMNBy similarity | 3 | |
Nucleotide bindingi | 141 – 143 | FMNBy similarity | 3 | |
Nucleotide bindingi | 346 – 347 | FMNBy similarity | 2 | |
Nucleotide bindingi | 368 – 369 | FMNBy similarity | 2 |
GO - Molecular functioni
- 3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione monooxygenase activity Source: UniProtKB-EC
- flavin adenine dinucleotide binding Source: UniProtKB
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen Source: MTBBASE
- oxidoreductase activity, acting on the CH-CH group of donors Source: InterPro
GO - Biological processi
- aromatic compound catabolic process Source: UniProtKB-KW
- cholesterol catabolic process Source: MTBBASE
- growth of symbiont in host Source: MTBBASE
- steroid biosynthetic process Source: UniProtKB
Keywordsi
Molecular function | Monooxygenase, Oxidoreductase |
Biological process | Aromatic hydrocarbons catabolism, Lipid degradation, Lipid metabolism, Steroid metabolism |
Ligand | FAD, Flavoprotein, FMN |
Enzyme and pathway databases
BioCyci | MetaCyc:G185E-7848-MONOMER |
UniPathwayi | UPA00062 |
Chemistry databases
SwissLipidsi | SLP:000001164 |
Names & Taxonomyi
Protein namesi | Recommended name: Flavin-dependent monooxygenase, oxygenase subunit HsaA (EC:1.14.14.121 Publication)Alternative name(s): 3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione 4-hydroxylase, oxygenase subunit 3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione monooxygenase |
Gene namesi | Name:hsaA1 Publication Ordered Locus Names:Rv3570c |
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 | Rv3570c |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000404501 | 1 – 394 | Flavin-dependent monooxygenase, oxygenase subunit HsaAAdd BLAST | 394 |
Proteomic databases
PaxDbi | P9WJA1 |
Expressioni
Inductioni
Induced by KstR.1 Publication
Interactioni
Subunit structurei
Homotetramer under anaerobic conditions. HsaAB monooxygenase consists of an oxygenase component HsaA and a reductase component HsaB.
1 PublicationProtein-protein interaction databases
STRINGi | 83332.Rv3570c |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P9WJA1 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Belongs to the HpaH/HsaA monooxygenase family.Curated
Phylogenomic databases
eggNOGi | COG1960, Bacteria |
OMAi | DVWHVVG |
PhylomeDBi | P9WJA1 |
Family and domain databases
Gene3Di | 1.10.540.10, 1 hit |
InterProi | View protein in InterPro IPR013107, Acyl-CoA_DH_C_dom IPR036250, AcylCo_DH-like_C IPR037069, AcylCoA_DH/ox_N_sf IPR009100, AcylCoA_DH/oxidase_NM_dom |
Pfami | View protein in Pfam PF08028, Acyl-CoA_dh_2, 1 hit |
SUPFAMi | SSF47203, SSF47203, 1 hit SSF56645, SSF56645, 1 hit |
i Sequence
Sequence statusi: Complete.
P9WJA1-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTSIQQRDAQ SVLAAIDNLL PEIRDRAQAT EDLRRLPDET VKALDDVGFF
60 70 80 90 100
TLLQPQQWGG LQCDPALFFE ATRRLASVCG STGWVSSIVG VHNWHLALFD
110 120 130 140 150
QRAQEEVWGE DPSTRISSSY APMGAGVVVD GGYLVNGSWN WSSGCDHASW
160 170 180 190 200
TFVGGPVIKD GRPVDFGSFL IPRSEYEIKD VWYVVGLRGT GSNTLVVKDV
210 220 230 240 250
FVPRHRFLSY KAMNDHTAGG LATNSAPVYK MPWGTMHPTT ISAPIVGMAY
260 270 280 290 300
GAYAAHVEHQ GKRVRAAFAG EKAKDDPFAK VRIAEAASDI DAAWRQLIGN
310 320 330 340 350
VSDEYALLAA GKEIPFELRA RARRDQVRAT GRSIASIDRL FEASGATALS
360 370 380 390
NEAPIQRFWR DAHAGRVHAA NDPERAYVIF GNHEFGLPPG DTMV
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP46393.1 |
PIRi | H70605 |
RefSeqi | NP_218087.1, NC_000962.3 WP_003900101.1, NZ_NVQJ01000014.1 |
Genome annotation databases
EnsemblBacteriai | CCP46393; CCP46393; Rv3570c |
GeneIDi | 23490155 887241 |
KEGGi | mtu:Rv3570c mtv:RVBD_3570c |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP46393.1 |
PIRi | H70605 |
RefSeqi | NP_218087.1, NC_000962.3 WP_003900101.1, NZ_NVQJ01000014.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3AFE | X-ray | 2.50 | A/B/C/D | 1-394 | [»] | |
3AFF | X-ray | 2.00 | A/B | 1-394 | [»] | |
SMRi | P9WJA1 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv3570c |
Chemistry databases
SwissLipidsi | SLP:000001164 |
Proteomic databases
PaxDbi | P9WJA1 |
Genome annotation databases
EnsemblBacteriai | CCP46393; CCP46393; Rv3570c |
GeneIDi | 23490155 887241 |
KEGGi | mtu:Rv3570c mtv:RVBD_3570c |
Organism-specific databases
TubercuListi | Rv3570c |
Phylogenomic databases
eggNOGi | COG1960, Bacteria |
OMAi | DVWHVVG |
PhylomeDBi | P9WJA1 |
Enzyme and pathway databases
UniPathwayi | UPA00062 |
BioCyci | MetaCyc:G185E-7848-MONOMER |
Family and domain databases
Gene3Di | 1.10.540.10, 1 hit |
InterProi | View protein in InterPro IPR013107, Acyl-CoA_DH_C_dom IPR036250, AcylCo_DH-like_C IPR037069, AcylCoA_DH/ox_N_sf IPR009100, AcylCoA_DH/oxidase_NM_dom |
Pfami | View protein in Pfam PF08028, Acyl-CoA_dh_2, 1 hit |
SUPFAMi | SSF47203, SSF47203, 1 hit SSF56645, SSF56645, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | HSAA_MYCTU | |
Accessioni | P9WJA1Primary (citable) accession number: P9WJA1 Secondary accession number(s): L0TCY6, P96852, Q7D595 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | December 2, 2020 | |
This is version 37 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, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families