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Protein

Sulfite reductase [NADPH] hemoprotein beta-component

Gene

cysI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.UniRule annotation

Catalytic activityi

H2S + 3 NADP+ + 3 H2O = sulfite + 3 NADPH.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • sirohemeUniRule annotation2 PublicationsNote: Binds 1 siroheme per subunit.UniRule annotation2 Publications
  • [4Fe-4S] clusterUniRule annotation2 PublicationsNote: Binds 1 [4Fe-4S] cluster per subunit.UniRule annotation2 Publications

Pathwayi: hydrogen sulfide biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes hydrogen sulfide from sulfite (NADPH route).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Sulfite reductase [NADPH] hemoprotein beta-component (cysI), Sulfite reductase [NADPH] flavoprotein alpha-component (cysJ)
This subpathway is part of the pathway hydrogen sulfide biosynthesis, which is itself part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes hydrogen sulfide from sulfite (NADPH route), the pathway hydrogen sulfide biosynthesis and in Sulfur metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi434Iron-sulfur (4Fe-4S)2 Publications1
Metal bindingi440Iron-sulfur (4Fe-4S)2 Publications1
Metal bindingi479Iron-sulfur (4Fe-4S)2 Publications1
Metal bindingi483Iron (siroheme axial ligand)2 Publications1
Metal bindingi483Iron-sulfur (4Fe-4S)2 Publications1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processAmino-acid biosynthesis, Cysteine biosynthesis
Ligand4Fe-4S, Heme, Iron, Iron-sulfur, Metal-binding, NADP

Enzyme and pathway databases

BioCyciEcoCyc:BETACOMP-MONOMER
MetaCyc:BETACOMP-MONOMER
UniPathwayiUPA00140; UER00207

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfite reductase [NADPH] hemoprotein beta-componentUniRule annotation (EC:1.8.1.2UniRule annotation)
Short name:
SiR-HPUniRule annotation
Short name:
SiRHPUniRule annotation
Gene namesi
Name:cysI
Ordered Locus Names:b2763, JW2733
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10190 cysI

Subcellular locationi

GO - Cellular componenti

  • sulfite reductase complex (NADPH) Source: EcoCyc

Pathology & Biotechi

Chemistry databases

DrugBankiDB02832 Siroheme

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001998962 – 570Sulfite reductase [NADPH] hemoprotein beta-componentAdd BLAST569

Proteomic databases

PaxDbiP17846
PRIDEiP17846

Interactioni

Subunit structurei

Alpha8-beta8. The alpha component is a flavoprotein, the beta component is a hemoprotein.UniRule annotation

Protein-protein interaction databases

BioGridi4262276, 162 interactors
DIPiDIP-9380N
IntActiP17846, 11 interactors
STRINGi316407.85675584

Structurei

Secondary structure

1570
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi82 – 85Combined sources4
Helixi87 – 89Combined sources3
Beta strandi90 – 92Combined sources3
Helixi93 – 106Combined sources14
Beta strandi107 – 109Combined sources3
Beta strandi112 – 114Combined sources3
Beta strandi120 – 122Combined sources3
Turni127 – 129Combined sources3
Helixi133 – 138Combined sources6
Turni139 – 141Combined sources3
Beta strandi143 – 145Combined sources3
Turni147 – 149Combined sources3
Helixi164 – 166Combined sources3
Helixi167 – 180Combined sources14
Turni205 – 207Combined sources3
Beta strandi218 – 221Combined sources4
Helixi230 – 232Combined sources3
Beta strandi233 – 253Combined sources21
Beta strandi272 – 278Combined sources7
Helixi279 – 281Combined sources3
Helixi282 – 296Combined sources15
Helixi302 – 304Combined sources3
Helixi307 – 314Combined sources8
Helixi316 – 327Combined sources12
Beta strandi347 – 350Combined sources4
Beta strandi352 – 354Combined sources3
Beta strandi355 – 360Combined sources6
Helixi363 – 365Combined sources3
Helixi375 – 385Combined sources11
Beta strandi387 – 392Combined sources6
Beta strandi398 – 404Combined sources7
Helixi405 – 407Combined sources3
Helixi408 – 417Combined sources10
Turni418 – 421Combined sources4
Helixi426 – 429Combined sources4
Beta strandi431 – 433Combined sources3
Turni437 – 439Combined sources3
Turni448 – 450Combined sources3
Helixi451 – 464Combined sources14
Beta strandi474 – 479Combined sources6
Helixi486 – 488Combined sources3
Beta strandi489 – 497Combined sources9
Beta strandi500 – 505Combined sources6
Beta strandi509 – 511Combined sources3
Beta strandi516 – 523Combined sources8
Helixi524 – 541Combined sources18
Helixi548 – 554Combined sources7
Helixi564 – 567Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AOPX-ray1.60A74-570[»]
2AOPX-ray1.75A74-570[»]
2GEPX-ray1.90A74-570[»]
3AOPX-ray2.10A74-570[»]
3GEOX-ray2.10A74-570[»]
4AOPX-ray1.80A74-570[»]
4G38X-ray1.56A1-570[»]
4G39X-ray2.40A1-570[»]
4GEPX-ray2.00A74-570[»]
4HTRX-ray1.60A64-570[»]
5AOPX-ray2.20A74-570[»]
5GEPX-ray2.10A74-570[»]
6GEPX-ray1.80A74-570[»]
7GEPX-ray2.40A74-570[»]
8GEPX-ray2.20A74-570[»]
ProteinModelPortaliP17846
SMRiP17846
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17846

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105ET1 Bacteria
COG0155 LUCA
HOGENOMiHOG000218418
InParanoidiP17846
KOiK00381
OMAiGKYNMYL
PhylomeDBiP17846

Family and domain databases

HAMAPiMF_01540 CysI, 1 hit
InterProiView protein in InterPro
IPR011786 CysI
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
PANTHERiPTHR11493:SF57 PTHR11493:SF57, 1 hit
PfamiView protein in Pfam
PF01077 NIR_SIR, 2 hits
PF03460 NIR_SIR_ferr, 2 hits
PRINTSiPR00397 SIROHAEM
SUPFAMiSSF55124 SSF55124, 2 hits
TIGRFAMsiTIGR02041 CysI, 1 hit
PROSITEiView protein in PROSITE
PS00365 NIR_SIR, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17846-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEKHPGPLV VEGKLTDAER MKHESNYLRG TIAEDLNDGL TGGFKGDNFL
60 70 80 90 100
LIRFHGMYQQ DDRDIRAERA EQKLEPRHAM LLRCRLPGGV ITTKQWQAID
110 120 130 140 150
KFAGENTIYG SIRLTNRQTF QFHGILKKNV KPVHQMLHSV GLDALATAND
160 170 180 190 200
MNRNVLCTSN PYESQLHAEA YEWAKKISEH LLPRTRAYAE IWLDQEKVAT
210 220 230 240 250
TDEEPILGQT YLPRKFKTTV VIPPQNDIDL HANDMNFVAI AENGKLVGFN
260 270 280 290 300
LLVGGGLSIE HGNKKTYART ASEFGYLPLE HTLAVAEAVV TTQRDWGNRT
310 320 330 340 350
DRKNAKTKYT LERVGVETFK AEVERRAGIK FEPIRPYEFT GRGDRIGWVK
360 370 380 390 400
GIDDNWHLTL FIENGRILDY PARPLKTGLL EIAKIHKGDF RITANQNLII
410 420 430 440 450
AGVPESEKAK IEKIAKESGL MNAVTPQREN SMACVSFPTC PLAMAEAERF
460 470 480 490 500
LPSFIDNIDN LMAKHGVSDE HIVMRVTGCP NGCGRAMLAE VGLVGKAPGR
510 520 530 540 550
YNLHLGGNRI GTRIPRMYKE NITEPEILAS LDELIGRWAK EREAGEGFGD
560 570
FTVRAGIIRP VLDPARDLWD
Length:570
Mass (Da):63,998
Last modified:January 23, 2007 - v4
Checksum:i03B41FEE6AB349C6
GO

Sequence cautioni

The sequence AAA23651 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAA68816 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti23H → L in AAA23651 (PubMed:2670946).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23008 Genomic DNA Translation: AAA23651.1 Different initiation.
U29579 Genomic DNA Translation: AAA69273.1
U00096 Genomic DNA Translation: AAC75805.1
AP009048 Genomic DNA Translation: BAE76840.1
Y07525 Genomic DNA Translation: CAA68816.1 Different initiation.
PIRiG65057 RDECSH
RefSeqiNP_417243.1, NC_000913.3
WP_001290679.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC75805; AAC75805; b2763
BAE76840; BAE76840; BAE76840
GeneIDi947231
KEGGiecj:JW2733
eco:b2763
PATRICifig|1411691.4.peg.3974

Similar proteinsi

Entry informationi

Entry nameiCYSI_ECOLI
AccessioniPrimary (citable) accession number: P17846
Secondary accession number(s): Q2MA66
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 167 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health