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Protein

Sulfite reductase [ferredoxin]

Gene

sir

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reduction of sulfite to sulfide, a step in the biosynthesis of sulfur-containing amino acids and cofactors.1 Publication

Catalytic activityi

Hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O = sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+.1 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 keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi417Iron-sulfur (4Fe-4S)1
Metal bindingi423Iron-sulfur (4Fe-4S)1
Metal bindingi463Iron-sulfur (4Fe-4S)1
Metal bindingi467Iron (siroheme axial ligand)1
Metal bindingi467Iron-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: Reactome
  • sulfite reductase activity Source: MTBBASE

GO - Biological processi

  • cysteine biosynthetic process from serine Source: Reactome
  • growth Source: MTBBASE
  • sulfate assimilation Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

4Fe-4S, Heme, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-6617-MONOMER.
ReactomeiR-MTU-936721. Cysteine synthesis from O-acetylserine.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfite reductase [ferredoxin] (EC:1.8.7.11 Publication)
Gene namesi
Name:sir
Synonyms:nirA
Ordered Locus Names:Rv2391
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv2391.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: MTBBASE
  • cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi69Y → A or F: Strong decrease in activity. 1 Publication1
Mutagenesisi161C → A or S: Strong decrease in activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001999521 – 555Sulfite reductase [ferredoxin]Add BLAST555

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki69 ↔ 1613'-(S-cysteinyl)-tyrosine (Tyr-Cys)

Keywords - PTMi

Thioether bond

Proteomic databases

PaxDbiP9WJ03.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv2391.

Structurei

Secondary structure

1555
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi15 – 17Combined sources3
Helixi25 – 29Combined sources5
Helixi30 – 32Combined sources3
Helixi35 – 37Combined sources3
Helixi38 – 44Combined sources7
Helixi46 – 49Combined sources4
Helixi51 – 53Combined sources3
Helixi56 – 60Combined sources5
Helixi62 – 66Combined sources5
Beta strandi68 – 72Combined sources5
Helixi78 – 80Combined sources3
Helixi83 – 85Combined sources3
Helixi86 – 89Combined sources4
Beta strandi90 – 99Combined sources10
Helixi101 – 103Combined sources3
Helixi107 – 120Combined sources14
Beta strandi124 – 127Combined sources4
Beta strandi133 – 138Combined sources6
Helixi140 – 142Combined sources3
Helixi143 – 151Combined sources9
Turni152 – 154Combined sources3
Beta strandi160 – 170Combined sources11
Turni172 – 176Combined sources5
Helixi185 – 195Combined sources11
Helixi199 – 201Combined sources3
Beta strandi208 – 216Combined sources9
Helixi220 – 222Combined sources3
Beta strandi223 – 232Combined sources10
Turni233 – 235Combined sources3
Beta strandi236 – 243Combined sources8
Beta strandi248 – 250Combined sources3
Beta strandi255 – 261Combined sources7
Helixi263 – 265Combined sources3
Helixi266 – 280Combined sources15
Helixi286 – 288Combined sources3
Helixi291 – 298Combined sources8
Helixi300 – 310Combined sources11
Beta strandi333 – 337Combined sources5
Beta strandi340 – 347Combined sources8
Beta strandi352 – 354Combined sources3
Helixi355 – 368Combined sources14
Beta strandi373 – 375Combined sources3
Beta strandi381 – 386Combined sources6
Helixi388 – 400Combined sources13
Beta strandi404 – 406Combined sources3
Helixi409 – 413Combined sources5
Beta strandi414 – 416Combined sources3
Helixi419 – 421Combined sources3
Helixi431 – 444Combined sources14
Helixi446 – 449Combined sources4
Beta strandi458 – 463Combined sources6
Helixi470 – 472Combined sources3
Beta strandi473 – 487Combined sources15
Beta strandi489 – 498Combined sources10
Beta strandi500 – 502Combined sources3
Turni518 – 520Combined sources3
Helixi521 – 534Combined sources14
Helixi542 – 548Combined sources7
Helixi551 – 554Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZJ8X-ray2.80A/B3-555[»]
1ZJ9X-ray2.90A/B3-555[»]
ProteinModelPortaliP9WJ03.
SMRiP9WJ03.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105ET1. Bacteria.
COG0155. LUCA.
KOiK00392.
OMAiVQSGMDN.

Family and domain databases

Gene3Di3.90.480.10. 2 hits.
InterProiIPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
IPR006066. NO2/SO3_Rdtase_FeS/sirohaem_BS.
[Graphical view]
PfamiPF01077. NIR_SIR. 2 hits.
PF03460. NIR_SIR_ferr. 2 hits.
[Graphical view]
PRINTSiPR00397. SIROHAEM.
SUPFAMiSSF55124. SSF55124. 2 hits.
PROSITEiPS00365. NIR_SIR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P9WJ03-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:555
Mass (Da):62,112
Last modified:April 16, 2014 - v1
Checksum:i68925CA37C131BC3
GO

Sequence cautioni

The sequence CCP45179 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP45179.1. Different initiation.
PIRiB70682.
RefSeqiNP_216907.1. NC_000962.3.

Genome annotation databases

EnsemblBacteriaiCCP45179; CCP45179; Rv2391.
GeneIDi885472.
KEGGimtu:Rv2391.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP45179.1. Different initiation.
PIRiB70682.
RefSeqiNP_216907.1. NC_000962.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZJ8X-ray2.80A/B3-555[»]
1ZJ9X-ray2.90A/B3-555[»]
ProteinModelPortaliP9WJ03.
SMRiP9WJ03.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2391.

Proteomic databases

PaxDbiP9WJ03.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP45179; CCP45179; Rv2391.
GeneIDi885472.
KEGGimtu:Rv2391.

Organism-specific databases

TubercuListiRv2391.

Phylogenomic databases

eggNOGiENOG4105ET1. Bacteria.
COG0155. LUCA.
KOiK00392.
OMAiVQSGMDN.

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-6617-MONOMER.
ReactomeiR-MTU-936721. Cysteine synthesis from O-acetylserine.

Family and domain databases

Gene3Di3.90.480.10. 2 hits.
InterProiIPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
IPR006066. NO2/SO3_Rdtase_FeS/sirohaem_BS.
[Graphical view]
PfamiPF01077. NIR_SIR. 2 hits.
PF03460. NIR_SIR_ferr. 2 hits.
[Graphical view]
PRINTSiPR00397. SIROHAEM.
SUPFAMiSSF55124. SSF55124. 2 hits.
PROSITEiPS00365. NIR_SIR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSIR_MYCTU
AccessioniPrimary (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: November 2, 2016
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Was identified as a high-confidence drug target.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.