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Database: UniProt
Entry: A1T053_PSYIN
LinkDB: A1T053_PSYIN
Original site: A1T053_PSYIN 
ID   A1T053_PSYIN            Unreviewed;       600 AA.
AC   A1T053;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   24-JAN-2024, entry version 115.
DE   RecName: Full=Sulfite reductase [NADPH] flavoprotein alpha-component {ECO:0000256|PIRNR:PIRNR000207};
DE            Short=SiR-FP {ECO:0000256|PIRNR:PIRNR000207};
DE            EC=1.8.1.2 {ECO:0000256|PIRNR:PIRNR000207};
GN   OrderedLocusNames=Ping_3434 {ECO:0000313|EMBL:ABM05118.1};
OS   Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=357804 {ECO:0000313|EMBL:ABM05118.1, ECO:0000313|Proteomes:UP000000639};
RN   [1] {ECO:0000313|EMBL:ABM05118.1, ECO:0000313|Proteomes:UP000000639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=37 {ECO:0000313|EMBL:ABM05118.1,
RC   ECO:0000313|Proteomes:UP000000639};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA   Richardson P.;
RT   "Complete sequence of Psychromonas ingrahamii 37.";
RL   Submitted (JAN-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.
CC       {ECO:0000256|PIRNR:PIRNR000207}.
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;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000207};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000207,
CC         ECO:0000256|PIRSR:PIRSR000207-1};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRNR:PIRNR000207,
CC       ECO:0000256|PIRSR:PIRSR000207-1};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000207,
CC         ECO:0000256|PIRSR:PIRSR000207-1};
CC       Note=Binds 1 FMN per subunit. {ECO:0000256|PIRNR:PIRNR000207,
CC       ECO:0000256|PIRSR:PIRSR000207-1};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen
CC       sulfide from sulfite (NADPH route): step 1/1.
CC       {ECO:0000256|PIRNR:PIRNR000207}.
CC   -!- SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein, the
CC       beta component is a hemoprotein. {ECO:0000256|PIRNR:PIRNR000207}.
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DR   EMBL; CP000510; ABM05118.1; -; Genomic_DNA.
DR   RefSeq; WP_011771670.1; NC_008709.1.
DR   AlphaFoldDB; A1T053; -.
DR   STRING; 357804.Ping_3434; -.
DR   KEGG; pin:Ping_3434; -.
DR   eggNOG; COG0369; Bacteria.
DR   HOGENOM; CLU_001570_17_7_6; -.
DR   OMA; QKRYQRD; -.
DR   OrthoDB; 9816402at2; -.
DR   UniPathway; UPA00140; UER00207.
DR   Proteomes; UP000000639; 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-EC.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd06199; SiR; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR010199; CysJ.
DR   InterPro; IPR003097; CysJ-like_FAD-binding.
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   NCBIfam; TIGR01931; cysJ; 1.
DR   PANTHER; PTHR19384:SF128; NADPH OXIDOREDUCTASE A; 1.
DR   PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
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; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|PIRNR:PIRNR000207};
KW   Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192,
KW   ECO:0000256|PIRNR:PIRNR000207};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW   ECO:0000256|PIRNR:PIRNR000207};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000207};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|PIRNR:PIRNR000207};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRNR:PIRNR000207};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000207};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000207};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000639};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000207}.
FT   DOMAIN          63..201
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          233..449
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   BINDING         116..119
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         152..161
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         321
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         386..389
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         404..406
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         420..423
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         520..521
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         526..530
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         562
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         600
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
SQ   SEQUENCE   600 AA;  66614 MW;  623713C2420D4313 CRC64;
     MAFNNISALT SPLSELQLSH LQQATTDLTP VQTAWISGYL AGISQTPATV ETVETAVSSG
     QHLTILFGSQ TGNCKGVAEQ LADQAAAKGI THTLISMADY KVKNIKDESH LIVVVSTNGE
     GEAPDDAIDL HEFLATKKAP KLDNLKFAVL ALGDSSYEFF CQTGKDFDQR LAALGATAIV
     DRLDADIDYE QQTPGWFEKV LNKVEQTLEK GGFVAPSKAT LETPLSVNKY DKKSPFAASL
     LTSQKITGAR SAKDVRHIEI DLEGSDLHYK VGDALGVWFE NDPQLVDALI KKLKLDPQEQ
     VKIDDKNISL KQALTESFEL TATHPAFVEG YAKLTKNKKL LTLAEDKNKL RDFANTHQII
     DVLSKKGSKA VTAEKFVTLL RHLSPRLYSI ASSQAEVEQE VHLTVAALTF ENEEGEVRQG
     GASGFLAHRL QEGQQVKVFI EDNHNFRLPS NPETPVIMVG PGTGIAPFRA FLQERDATEA
     TGKNWLFFGE QTFTEDFLYQ TEWQGFLKSG LLTNLDLAFS RDQAEKIYVQ DRLKEHAHEI
     YQWLQEGAHF YVCGDANRMA KDVQQTLIEI IGSQGKKSLE DAEQYLTELR QAKRYQRDVY
//
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