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CYSJ_NEIMF
ID   CYSJ_NEIMF              Reviewed;         604 AA.
AC   A1KU06;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=NMC1092;
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS   15464 / FAM18).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=272831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA   Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA   Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA   Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(2007).
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; AM421808; CAM10347.1; -; Genomic_DNA.
DR   RefSeq; WP_002224539.1; NC_008767.1.
DR   AlphaFoldDB; A1KU06; -.
DR   SMR; A1KU06; -.
DR   EnsemblBacteria; CAM10347; CAM10347; NMC1092.
DR   KEGG; nmc:NMC1092; -.
DR   HOGENOM; CLU_001570_17_7_4; -.
DR   OMA; QKRYQRD; -.
DR   OrthoDB; 707164at2; -.
DR   UniPathway; UPA00140; UER00207.
DR   Proteomes; UP000002286; 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; Transport.
FT   CHAIN           1..604
FT                   /note="Sulfite reductase [NADPH] flavoprotein alpha-
FT                   component"
FT                   /id="PRO_0000292969"
FT   DOMAIN          66..204
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   DOMAIN          239..453
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   REGION          212..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         72..77
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         119..122
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         155..164
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         327
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         361
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         391..394
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         409..411
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         424..427
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         524..525
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         530..534
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         566
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         604
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
SQ   SEQUENCE   604 AA;  66179 MW;  DF731CD89E5791BD CRC64;
     MSEHDMQNTN PPLPPLPPEI TQLLSGLDAA QWAWLSGYAW AKAGNGASAG LPALQTALPA
     AEPFSVTVLS ASQTGNAKSV ADKASDSLEA AGIQVRRAEL KDYKAKNIAD ERRLLLVTST
     QGEGEPPEEA VVLHKLLNGK KAPKLDKLQF AVLGLGDSSY PNFCRAGKDF DRRFEELGAK
     RLLERVDADL DFAAAADGWT GRIVARLKEE AAKNRATPAP QTTPPAGLQT APDGRYCKAD
     PFPAALLANQ KITARQSDKD VRHIEIDLSG SDLHYLPGDA LGVWFDNDPA LVREILDLLG
     IDPATEIQAG GKTLPVASAL LSHFELTQNT PAFVKGYAPF ADDDELDRIA ADNAVLQGFV
     QSTPIADVLH RFPAKLTAEQ FAGLLRPLAP RLYSISSSQA EVGDEVHLTV GAVRFEHEGR
     ARAGGASGFL ADRLEEDGTV RVFVERNDGF RLPEDSRKPI VMIGSGTGVA PFRAFVQQRA
     AENAEGKNWL IFGNPHFARD FLYQTEWQQF AKDGFLHRYD FAWSRDQEEK IYVQDKIREQ
     AEGLWQWLQE GAHIYVCGDA AKMAKDVEAA LLDVIIGAGH LDEEGAEEYL DMLREEKRYQ
     RDVY
 
 
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