CYSJ_CITK8
ID CYSJ_CITK8 Reviewed; 601 AA.
AC A8ANX1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Sulfite reductase [NADPH] flavoprotein alpha-component {ECO:0000255|HAMAP-Rule:MF_01541};
DE Short=SiR-FP {ECO:0000255|HAMAP-Rule:MF_01541};
DE EC=1.8.1.2 {ECO:0000255|HAMAP-Rule:MF_01541};
GN Name=cysJ {ECO:0000255|HAMAP-Rule:MF_01541}; OrderedLocusNames=CKO_04119;
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the sulfite reductase complex that catalyzes the
CC 6-electron reduction of sulfite to sulfide. This is one of several
CC activities required for the biosynthesis of L-cysteine from sulfate.
CC The flavoprotein component catalyzes the electron flow from NADPH ->
CC FAD -> FMN to the hemoprotein component. {ECO:0000255|HAMAP-
CC Rule:MF_01541}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH +
CC sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01541};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01541};
CC Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_01541};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01541};
CC Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01541};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen
CC sulfide from sulfite (NADPH route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01541}.
CC -!- SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein, the
CC beta component is a hemoprotein. {ECO:0000255|HAMAP-Rule:MF_01541}.
CC -!- SIMILARITY: Belongs to the NADPH-dependent sulphite reductase
CC flavoprotein subunit CysJ family. {ECO:0000255|HAMAP-Rule:MF_01541}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
CC family. {ECO:0000255|HAMAP-Rule:MF_01541}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC pyridine nucleotide cytochrome reductase family. {ECO:0000255|HAMAP-
CC Rule:MF_01541}.
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DR EMBL; CP000822; ABV15185.1; -; Genomic_DNA.
DR RefSeq; WP_012134873.1; NC_009792.1.
DR AlphaFoldDB; A8ANX1; -.
DR SMR; A8ANX1; -.
DR STRING; 290338.CKO_04119; -.
DR EnsemblBacteria; ABV15185; ABV15185; CKO_04119.
DR GeneID; 45137754; -.
DR KEGG; cko:CKO_04119; -.
DR HOGENOM; CLU_001570_17_7_6; -.
DR OMA; QKRYQRD; -.
DR OrthoDB; 707164at2; -.
DR UniPathway; UPA00140; UER00207.
DR Proteomes; UP000008148; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.990.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR HAMAP; MF_01541; CysJ; 1.
DR InterPro; IPR010199; CysJ.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR029758; CysJ_Proteobact.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF000207; SiR-FP_CysJ; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52218; SSF52218; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR TIGRFAMs; TIGR01931; cysJ; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cysteine biosynthesis; Electron transport; FAD;
KW Flavoprotein; FMN; NADP; Oxidoreductase; Reference proteome; Transport.
FT CHAIN 1..601
FT /note="Sulfite reductase [NADPH] flavoprotein alpha-
FT component"
FT /id="PRO_1000087631"
FT DOMAIN 64..202
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT DOMAIN 236..450
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT BINDING 70..75
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT BINDING 117..120
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT BINDING 153..162
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT BINDING 324
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT BINDING 358
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT BINDING 388..391
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT BINDING 406..408
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT BINDING 412
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT BINDING 421..424
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT BINDING 521..522
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT BINDING 527..531
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT BINDING 563
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT BINDING 601
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
SQ SEQUENCE 601 AA; 66119 MW; 93406AEFEFF5701A CRC64;
MTTQAPPSAL LPLNPEQLAR LQAATTDLSP TQLAWVSGYF WGMLNQQPGT LAATPAPVAE
MPGITLISAS QTGNARRVAE ALRDDLLAAK LSVTLVNAGD YKFKQIANEK LLVVVASTQG
EGEPPEEAVA LRKFLFSKKA PKLDNTAFAV FGLGDTSYEF FCQAGKDFDS KLAELGGERL
LDRVDADVEY QAAAQEWRAR VVDVLKARAP SASAAQVAVA ATGAVNDVHS SPYTKEAPLS
ASLAVNQKIT GRDSEKDVRH IEIDLGDSGL RYQPGDALGV WYQNDPELVK EIVELVWLKG
TEPVTVNGKV LPLAEALQWH FELTVNTANI VENYATLTRS ESLLPLVGDK AQLQHYAATT
PIVDMLRFSP AQLDADALVG LLRPLTPRLY SIASSQAEVE SEVHITVGAV RYEIEGRARA
GGASSFLADR VEEEGEVRVF IEHNDNFRLP ANPETPVIMI GPGTGIAPFR AFMQQRAADE
APGKNWLFFG NPHFTEDFLY QVEWQRYVKE GVLSRIDLAW SRDQKEKIYV QDKLREQGAE
LWRWINDGAH IYVCGDANCM AKDVEQALLE VIAEFGGMDA EAADEFLSEL RVERRYQRDV
Y
