ID K2PYJ0_9FLAO Unreviewed; 606 AA.
AC K2PYJ0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=Sulfite reductase [NADPH] flavoprotein alpha-component {ECO:0000313|EMBL:EKF56534.1};
GN ORFNames=I215_03398 {ECO:0000313|EMBL:EKF56534.1};
OS Galbibacter marinus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Galbibacter.
OX NCBI_TaxID=555500 {ECO:0000313|EMBL:EKF56534.1, ECO:0000313|Proteomes:UP000007364};
RN [1] {ECO:0000313|EMBL:EKF56534.1, ECO:0000313|Proteomes:UP000007364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ck-I2-15 {ECO:0000313|Proteomes:UP000007364};
RX PubMed=23209227; DOI=10.1128/JB.01852-12;
RA Lai Q., Li C., Shao Z.;
RT "Genome Sequence of Galbibacter marinum Type Strain ck-I2-15.";
RL J. Bacteriol. 194:6973-6973(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000207-1};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000207-1};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|PIRSR:PIRSR000207-1};
CC Note=Binds 1 FMN per subunit. {ECO:0000256|PIRSR:PIRSR000207-1};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKF56534.1}.
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DR EMBL; AMSG01000002; EKF56534.1; -; Genomic_DNA.
DR RefSeq; WP_008990553.1; NZ_AMSG01000002.1.
DR AlphaFoldDB; K2PYJ0; -.
DR STRING; 555500.I215_03398; -.
DR PATRIC; fig|555500.3.peg.705; -.
DR eggNOG; COG0369; Bacteria.
DR OrthoDB; 9789468at2; -.
DR Proteomes; UP000007364; Unassembled WGS sequence.
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:InterPro.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
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 Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000207-1};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRSR:PIRSR000207-1};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR000207-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007364};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 72..210
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 242..455
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 125..128
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 161..170
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 330
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 393..396
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 417
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 426..429
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 526..527
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 532..536
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 568
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 606
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
SQ SEQUENCE 606 AA; 67360 MW; 5A0E5DCD65AC2E86 CRC64;
MELHKGLGRG PFNDSQAERL SNVLSELDAD QLHWLSGYIS GITQTTSFGP ATTTSQEVVS
VAAKLESKPQ NITILFGSHT GHSEALSADL AEKAKQLGIE VSVSDMASFK TRDLKKIENL
AIIVSTHGLG EPPVQAEDLY KYLHGKKAPN LSHINFSVLA LGDSSYADFC QTGKDFDAVL
EKLGAKRILD RQDCDVDYED PAETWQEAFL DSLTQNSNQA SLTEKVQANG TPVGSKTVYS
KKNLFEATIL EKINLNGKGS SKETIHIELD LEDSGITYEP GDALGVYGSN SPKLTQAVLE
ATKLSGDQLV TTHDGEKTLH DALTYDYELT PLTKSTLQKY AELTDSSKLK DILNGSDIQE
YLLGRDILDL INETPYELSA EEFISTLRKN TARMYSIASS QEAVENEVHL LVSVVRYNAL
GRDKEGHCST TLADRLEVDD KVKVFVDKNT RFKLPSDPES PIIMVGPGTG VAPFRAFMQQ
IEVSQKKNPS WLFFGDRNFT TDFLYQTEWQ QYLNEGVLTK ADVAFSRDQA NKQYVQDRMI
ENGKELYEWL EKGAHFYVCG DASRMAKDVD SALKEIIQQQ GGLSLEKTEA YIKNLQLSNR
YQTDIY
//
