ID K6ZQH7_9ALTE Unreviewed; 237 AA.
AC K6ZQH7;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=NAD(P)H-flavin reductase {ECO:0000313|EMBL:GAC32537.1};
GN Name=fre {ECO:0000313|EMBL:GAC32537.1};
GN ORFNames=GPLA_1623 {ECO:0000313|EMBL:GAC32537.1};
OS Paraglaciecola polaris LMG 21857.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1129793 {ECO:0000313|EMBL:GAC32537.1, ECO:0000313|Proteomes:UP000006322};
RN [1] {ECO:0000313|EMBL:GAC32537.1, ECO:0000313|Proteomes:UP000006322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21857 {ECO:0000313|EMBL:GAC32537.1,
RC ECO:0000313|Proteomes:UP000006322};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- SIMILARITY: Belongs to the Fre/LuxG FAD/NAD(P) flavoprotein
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00038177}.
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:GAC32537.1}.
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DR EMBL; BAER01000041; GAC32537.1; -; Genomic_DNA.
DR RefSeq; WP_007104325.1; NZ_BAER01000041.1.
DR AlphaFoldDB; K6ZQH7; -.
DR STRING; 1129793.GPLA_1623; -.
DR OrthoDB; 9806195at2; -.
DR Proteomes; UP000006322; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR CDD; cd06189; flavin_oxioreductase; 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; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354:SF7; NAD(P)H-FLAVIN REDUCTASE; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Luminescence {ECO:0000256|ARBA:ARBA00023223}.
FT DOMAIN 1..99
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 237 AA; 26362 MW; 711584E0412FC2EB CRC64;
MHHTLCKVDS IVALNPVVSL VTLTPQQPFT YQAGQYLKVV MDEGDQRPFS IATAPRKDGK
IQLHIGAEPG NSYAGEVLDR MRQDNEITVS GGLGNAFART DTSMPTILLA GGTGFSYTQA
ILHEMLAAAE HIKGHKDPVF LYWGTRSTAD MYAYDELIAL EKQHAHFTFI PVVEHPGHQW
AGKTGWVHKA VLEDFVSLEP YRVYVAGRFE MAGVAREEFH QKGLILKNLY GDAFEFI
//
