ID CYSI_ZYMMO Reviewed; 570 AA.
AC Q5NRM2;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 01-MAY-2013, entry version 60.
DE RecName: Full=Sulfite reductase [NADPH] hemoprotein beta-component;
DE Short=SiR-HP;
DE Short=SiRHP;
DE EC=1.8.1.2;
GN Name=cysI; OrderedLocusNames=ZMO0008;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J.,
RA Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M.,
RA Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y.,
RA Kang H.L., Lee S.Y., Lee K.J., Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
CC -!- FUNCTION: Component of the sulfite reductase complex that
CC catalyzes the 6-electron reduction of sulfite to sulfide. This is
CC one of several activities required for the biosynthesis of L-
CC cysteine from sulfate (By similarity).
CC -!- CATALYTIC ACTIVITY: H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3
CC NADPH.
CC -!- COFACTOR: Binds 1 siroheme per subunit (By similarity).
CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity).
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis;
CC hydrogen sulfide from sulfite (NADPH route): step 1/1.
CC -!- SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein,
CC the beta component is a hemoprotein (By similarity).
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S
CC domain family.
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DR EMBL; AE008692; AAV88632.1; -; Genomic_DNA.
DR RefSeq; YP_161743.1; NC_006526.2.
DR ProteinModelPortal; Q5NRM2; -.
DR SMR; Q5NRM2; 81-570.
DR STRING; 264203.ZMO0008; -.
DR EnsemblBacteria; AAV88632; AAV88632; ZMO0008.
DR GeneID; 3189461; -.
DR KEGG; zmo:ZMO0008; -.
DR PATRIC; 32565380; VBIZymMob102260_0008.
DR eggNOG; COG0155; -.
DR HOGENOM; HOG000218418; -.
DR KO; K00381; -.
DR OMA; RNVMAPA; -.
DR ProtClustDB; PRK13504; -.
DR UniPathway; UPA00140; UER00207.
DR GO; GO:0009337; C:sulfite reductase complex (NADPH); IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:HAMAP.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:HAMAP.
DR GO; GO:0000103; P:sulfate assimilation; IEA:HAMAP.
DR Gene3D; 3.90.480.10; -; 2.
DR HAMAP; MF_01540; CysI; 1; -.
DR InterPro; IPR011786; CysI.
DR InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR Pfam; PF01077; NIR_SIR; 2.
DR Pfam; PF03460; NIR_SIR_ferr; 2.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF55124; NiR_SiRalpha_1/3; 2.
DR TIGRFAMs; TIGR02041; CysI; 1.
DR PROSITE; PS00365; NIR_SIR; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Amino-acid biosynthesis; Complete proteome;
KW Cysteine biosynthesis; Heme; Iron; Iron-sulfur; Metal-binding; NADP;
KW Oxidoreductase.
FT CHAIN 1 570 Sulfite reductase [NADPH] hemoprotein
FT beta-component.
FT /FTId=PRO_0000199919.
FT METAL 434 434 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 440 440 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 479 479 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 483 483 Iron (siroheme axial ligand) (By
FT similarity).
FT METAL 483 483 Iron-sulfur (4Fe-4S) (By similarity).
SQ SEQUENCE 570 AA; 64064 MW; BA050FC80FC53326 CRC64;
MTQKHPQTLV VDAPLSDAER LKRESNFLRG TIAEDLNDGL TGGFNGDNST LIRFHGMYQQ
DDRDIRAERA EEKLEPRYAM MLRCRLPGGI ISPEQWLKMD SFASEKTLYG SIRLTNRQTF
QFHGILKKDL KTVHHLLHES GLDSLATAND VNRNVLCTSN PVESDLHAEA YEWAKKISEH
LLPQTHAYAE IWLDQEKLAT TDQEPILGAT YLPRKFKTTV VIPPQNDVDI YANDLNFIAI
SENDQLVGFN VLIGGGLSIT IGDKTTHPGV AKDIGYIEKE KVLAVAEAVV TTQRDWGNRS
NRKNARLRYT LERVGLDVFK AEVEKRAGVT FEASRPFTLT GRGDRFGWVK GIDNQWHLTL
FVENGRLLDY PHRPLKSGIA EIAKVHKGDF RLTANQNLIV AGVSEEDKDT IEKIARDHGL
LENISELRKN SMACVSFPTC PLAMAEAERF LPNFLTKVEA VMTKYDIADE YIVFRTTGCP
NNCGRSLLAE IGLVGRAIGR YNLYIGGDRV GTRIPRLFRE NITEDEILSE VDSLIGRWAK
ERDGKEAFGD FVVRAGIVKA VTDPAIDFYD
//
