UniProtKB - P9WJ03 (SIR_MYCTU)
Protein
Sulfite reductase [ferredoxin]
Gene
sir
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
Catalyzes the reduction of sulfite to sulfide, a step in the biosynthesis of sulfur-containing amino acids and cofactors.1 Publication
Miscellaneous
Was identified as a high-confidence drug target.
Catalytic activityi
- 3 H2O + hydrogen sulfide + 6 oxidized [2Fe-2S]-[ferredoxin] = 7 H+ + 6 reduced [2Fe-2S]-[ferredoxin] + sulfite1 PublicationEC:1.8.7.11 Publication
Cofactori
Protein has several cofactor binding sites:- siroheme1 PublicationNote: Binds 1 siroheme per subunit.1 Publication
- [4Fe-4S] cluster1 PublicationNote: Binds 1 [4Fe-4S] cluster per subunit.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 417 | Iron-sulfur (4Fe-4S) | 1 | |
Metal bindingi | 423 | Iron-sulfur (4Fe-4S) | 1 | |
Metal bindingi | 463 | Iron-sulfur (4Fe-4S) | 1 | |
Metal bindingi | 467 | Iron (siroheme axial ligand) | 1 | |
Metal bindingi | 467 | Iron-sulfur (4Fe-4S) | 1 |
GO - Molecular functioni
- 4 iron, 4 sulfur cluster binding Source: MTBBASE
- heme binding Source: InterPro
- metal ion binding Source: UniProtKB-KW
- sulfite reductase (ferredoxin) activity Source: UniProtKB-EC
- sulfite reductase activity Source: MTBBASE
GO - Biological processi
- cysteine biosynthetic process from serine Source: Reactome
- sulfate assimilation Source: MTBBASE
Keywordsi
Molecular function | Oxidoreductase |
Ligand | 4Fe-4S, Heme, Iron, Iron-sulfur, Metal-binding |
Enzyme and pathway databases
BioCyci | MTBH37RV:G185E-6617-MONOMER |
Reactomei | R-MTU-936721 Cysteine synthesis from O-acetylserine |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:sir Synonyms:nirA Ordered Locus Names:Rv2391 |
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 | Rv2391 |
Subcellular locationi
GO - Cellular componenti
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 69 | Y → A or F: Strong decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 161 | C → A or S: Strong decrease in activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000199952 | 1 – 555 | Sulfite reductase [ferredoxin]Add BLAST | 555 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Cross-linki | 69 ↔ 161 | 3'-(S-cysteinyl)-tyrosine (Tyr-Cys) |
Keywords - PTMi
Thioether bondProteomic databases
PaxDbi | P9WJ03 |
Interactioni
Subunit structurei
Monomer.
1 PublicationProtein-protein interaction databases
STRINGi | 83332.Rv2391 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P9WJ03 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.Curated
Phylogenomic databases
eggNOGi | ENOG4105ET1 Bacteria COG0155 LUCA |
KOi | K00392 |
OMAi | GKYNMYL |
Family and domain databases
InterProi | View protein in InterPro IPR005117 NiRdtase/SiRdtase_haem-b_fer IPR036136 Nit/Sulf_reduc_fer-like_dom_sf IPR006067 NO2/SO3_Rdtase_4Fe4S_dom IPR006066 NO2/SO3_Rdtase_FeS/sirohaem_BS |
Pfami | View protein in Pfam PF01077 NIR_SIR, 2 hits PF03460 NIR_SIR_ferr, 2 hits |
PRINTSi | PR00397 SIROHAEM |
SUPFAMi | SSF55124 SSF55124, 2 hits |
PROSITEi | View protein in PROSITE PS00365 NIR_SIR, 1 hit |
i Sequence
Sequence statusi: Complete.
P9WJ03-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTTARPAKAR NEGQWALGHR EPLNANEELK KAGNPLDVRE RIENIYAKQG
60 70 80 90 100
FDSIDKTDLR GRFRWWGLYT QREQGYDGTW TGDDNIDKLE AKYFMMRVRC
110 120 130 140 150
DGGALSAAAL RTLGQISTEF ARDTADISDR QNVQYHWIEV ENVPEIWRRL
160 170 180 190 200
DDVGLQTTEA CGDCPRVVLG SPLAGESLDE VLDPTWAIEE IVRRYIGKPD
210 220 230 240 250
FADLPRKYKT AISGLQDVAH EINDVAFIGV NHPEHGPGLD LWVGGGLSTN
260 270 280 290 300
PMLAQRVGAW VPLGEVPEVW AAVTSVFRDY GYRRLRAKAR LKFLIKDWGI
310 320 330 340 350
AKFREVLETE YLKRPLIDGP APEPVKHPID HVGVQRLKNG LNAVGVAPIA
360 370 380 390 400
GRVSGTILTA VADLMARAGS DRIRFTPYQK LVILDIPDAL LDDLIAGLDA
410 420 430 440 450
LGLQSRPSHW RRNLMACSGI EFCKLSFAET RVRAQHLVPE LERRLEDINS
460 470 480 490 500
QLDVPITVNI NGCPNSCARI QIADIGFKGQ MIDDGHGGSV EGFQVHLGGH
510 520 530 540 550
LGLDAGFGRK LRQHKVTSDE LGDYIDRVVR NFVKHRSEGE RFAQWVIRAE
EDDLR
Sequence cautioni
The sequence CCP45179 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP45179.1 Different initiation. |
PIRi | B70682 |
RefSeqi | NP_216907.1, NC_000962.3 |
Genome annotation databases
EnsemblBacteriai | CCP45179; CCP45179; Rv2391 |
GeneIDi | 885472 |
KEGGi | mtu:Rv2391 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP45179.1 Different initiation. |
PIRi | B70682 |
RefSeqi | NP_216907.1, NC_000962.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1ZJ8 | X-ray | 2.80 | A/B | 3-555 | [»] | |
1ZJ9 | X-ray | 2.90 | A/B | 3-555 | [»] | |
SMRi | P9WJ03 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv2391 |
Proteomic databases
PaxDbi | P9WJ03 |
Genome annotation databases
EnsemblBacteriai | CCP45179; CCP45179; Rv2391 |
GeneIDi | 885472 |
KEGGi | mtu:Rv2391 |
Organism-specific databases
TubercuListi | Rv2391 |
Phylogenomic databases
eggNOGi | ENOG4105ET1 Bacteria COG0155 LUCA |
KOi | K00392 |
OMAi | GKYNMYL |
Enzyme and pathway databases
BioCyci | MTBH37RV:G185E-6617-MONOMER |
Reactomei | R-MTU-936721 Cysteine synthesis from O-acetylserine |
Family and domain databases
InterProi | View protein in InterPro IPR005117 NiRdtase/SiRdtase_haem-b_fer IPR036136 Nit/Sulf_reduc_fer-like_dom_sf IPR006067 NO2/SO3_Rdtase_4Fe4S_dom IPR006066 NO2/SO3_Rdtase_FeS/sirohaem_BS |
Pfami | View protein in Pfam PF01077 NIR_SIR, 2 hits PF03460 NIR_SIR_ferr, 2 hits |
PRINTSi | PR00397 SIROHAEM |
SUPFAMi | SSF55124 SSF55124, 2 hits |
PROSITEi | View protein in PROSITE PS00365 NIR_SIR, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | SIR_MYCTU | |
Accessioni | P9WJ03Primary (citable) accession number: P9WJ03 Secondary accession number(s): L0T9H3, P71753, Q7D781 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | October 16, 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, 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 - PDB cross-references
Index of Protein Data Bank (PDB) cross-references