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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi417 – 4171Iron-sulfur (4Fe-4S)
Metal bindingi423 – 4231Iron-sulfur (4Fe-4S)
Metal bindingi463 – 4631Iron-sulfur (4Fe-4S)
Metal bindingi467 – 4671Iron (siroheme axial ligand)
Metal bindingi467 – 4671Iron-sulfur (4Fe-4S)

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
  • sulfur amino acid metabolic process Source: Reactome
  • sulfur compound metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

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

Enzyme and pathway databases

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi69 – 691Y → A or F: Strong decrease in activity. 1 Publication
Mutagenesisi161 – 1611C → A or S: Strong decrease in activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 555555Sulfite reductase [ferredoxin]PRO_0000199952Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

1
555
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 173Combined sources
Helixi25 – 295Combined sources
Helixi30 – 323Combined sources
Helixi35 – 373Combined sources
Helixi38 – 447Combined sources
Helixi46 – 494Combined sources
Helixi51 – 533Combined sources
Helixi56 – 605Combined sources
Helixi62 – 665Combined sources
Beta strandi68 – 725Combined sources
Helixi78 – 803Combined sources
Helixi83 – 853Combined sources
Helixi86 – 894Combined sources
Beta strandi90 – 9910Combined sources
Helixi101 – 1033Combined sources
Helixi107 – 12014Combined sources
Beta strandi124 – 1274Combined sources
Beta strandi133 – 1386Combined sources
Helixi140 – 1423Combined sources
Helixi143 – 1519Combined sources
Turni152 – 1543Combined sources
Beta strandi160 – 17011Combined sources
Turni172 – 1765Combined sources
Helixi185 – 19511Combined sources
Helixi199 – 2013Combined sources
Beta strandi208 – 2169Combined sources
Helixi220 – 2223Combined sources
Beta strandi223 – 23210Combined sources
Turni233 – 2353Combined sources
Beta strandi236 – 2438Combined sources
Beta strandi248 – 2503Combined sources
Beta strandi255 – 2617Combined sources
Helixi263 – 2653Combined sources
Helixi266 – 28015Combined sources
Helixi286 – 2883Combined sources
Helixi291 – 2988Combined sources
Helixi300 – 31011Combined sources
Beta strandi333 – 3375Combined sources
Beta strandi340 – 3478Combined sources
Beta strandi352 – 3543Combined sources
Helixi355 – 36814Combined sources
Beta strandi373 – 3753Combined sources
Beta strandi381 – 3866Combined sources
Helixi388 – 40013Combined sources
Beta strandi404 – 4063Combined sources
Helixi409 – 4135Combined sources
Beta strandi414 – 4163Combined sources
Helixi419 – 4213Combined sources
Helixi431 – 44414Combined sources
Helixi446 – 4494Combined sources
Beta strandi458 – 4636Combined sources
Helixi470 – 4723Combined sources
Beta strandi473 – 48715Combined sources
Beta strandi489 – 49810Combined sources
Beta strandi500 – 5023Combined sources
Turni518 – 5203Combined sources
Helixi521 – 53414Combined sources
Helixi542 – 5487Combined sources
Helixi551 – 5544Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZJ8X-ray2.80A/B3-555[»]
1ZJ9X-ray2.90A/B3-555[»]
ProteinModelPortaliP9WJ03.
SMRiP9WJ03. Positions 10-555.
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 CCP45179.1 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
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZJ8X-ray2.80A/B3-555[»]
1ZJ9X-ray2.90A/B3-555[»]
ProteinModelPortaliP9WJ03.
SMRiP9WJ03. Positions 10-555.
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

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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. "targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
    Raman K., Yeturu K., Chandra N.
    BMC Syst. Biol. 2:109-109(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.
  4. "Siroheme- and [Fe4-S4]-dependent NirA from Mycobacterium tuberculosis is a sulfite reductase with a covalent Cys-Tyr bond in the active site."
    Schnell R., Sandalova T., Hellman U., Lindqvist Y., Schneider G.
    J. Biol. Chem. 280:27319-27328(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF TYR-69 AND CYS-161.
    Strain: ATCC 25618 / H37Rv.

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 11, 2015
This is version 18 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.