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Database: UniProt
Entry: A0A0F5VET6_9GAMM
LinkDB: A0A0F5VET6_9GAMM
Original site: A0A0F5VET6_9GAMM 
ID   A0A0F5VET6_9GAMM        Unreviewed;       461 AA.
AC   A0A0F5VET6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:KKD00568.1};
GN   ORFNames=KY46_07860 {ECO:0000313|EMBL:KKD00568.1};
OS   Photobacterium halotolerans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=265726 {ECO:0000313|EMBL:KKD00568.1, ECO:0000313|Proteomes:UP000033633};
RN   [1] {ECO:0000313|EMBL:KKD00568.1, ECO:0000313|Proteomes:UP000033633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MELD1 {ECO:0000313|EMBL:KKD00568.1,
RC   ECO:0000313|Proteomes:UP000033633};
RA   Mathew D.C., Huang C.-C.;
RT   "Mercury Reductase activity and rhizosphere competence traits in the genome
RT   of root associated Photobacterium halotolerans MELD1.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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:KKD00568.1}.
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DR   EMBL; JWYV01000004; KKD00568.1; -; Genomic_DNA.
DR   RefSeq; WP_046220117.1; NZ_JWYV01000004.1.
DR   AlphaFoldDB; A0A0F5VET6; -.
DR   STRING; 265726.KY46_07860; -.
DR   PATRIC; fig|265726.11.peg.3641; -.
DR   OrthoDB; 9775082at2; -.
DR   Proteomes; UP000033633; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.20; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR   PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033633}.
FT   DOMAIN          39..209
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   461 AA;  50694 MW;  28FCB1EFFABADDF9 CRC64;
     MSQLEAASID KFRVHFQGKV IVPKDDEYDE VRQIWNAMID RKPALIARCV SAECVLQAVN
     FAREHDLLLS VRGGGHNIAG NAVCDGGIMI DLSLMKGVHV NPNTRKVMVE PGCTLGDVDA
     AVQKYGLATP FGINSTTGVS GLTLGGGFGW LSRLYGMTID NLLSAHVVTA KGTQVKASET
     ENADLFWGLR GGGGNFGIVT SFEFQLHPVG PDVLSGLIVF PFEQAKSVLT QFARFTESMP
     EALNVWMVTR KAPPLPFLPE TVHGREMIAL ALCYFGDPDE GEKLIAPLRS FGTPYGEHIG
     VQPYVAWQQA FDPLLAPGAR NYWKSHNFTH LSDDVLEVLI EFAGKLPSPH CEIFIGTIGG
     QTEKVSPDAM AYASRDARYV MNVHGRWETA AEDEVCIAWA REFFTQSQPF ASAGAYINFL
     TQDESDRIAF AYGEAYKRLV ALKAKYDPHN LFRMNQNIKP E
//
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