ID A0A0M7B871_9RHOB Unreviewed; 464 AA.
AC A0A0M7B871;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Putative FAD-linked oxidoreductase {ECO:0000313|EMBL:CUH38910.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:CUH38910.1};
GN ORFNames=JSE7799_01629 {ECO:0000313|EMBL:CUH38910.1};
OS Jannaschia seosinensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=313367 {ECO:0000313|EMBL:CUH38910.1, ECO:0000313|Proteomes:UP000049455};
RN [1] {ECO:0000313|EMBL:CUH38910.1, ECO:0000313|Proteomes:UP000049455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7799 {ECO:0000313|EMBL:CUH38910.1,
RC ECO:0000313|Proteomes:UP000049455};
RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL Submitted (SEP-2015) 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 FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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DR EMBL; CYPR01000101; CUH38910.1; -; Genomic_DNA.
DR RefSeq; WP_055663170.1; NZ_CYPR01000101.1.
DR AlphaFoldDB; A0A0M7B871; -.
DR STRING; 313367.JSE7799_01629; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000049455; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
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; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 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 Oxidoreductase {ECO:0000313|EMBL:CUH38910.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000049455}.
FT DOMAIN 41..219
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 464 AA; 49732 MW; 135DBD96A798B663 CRC64;
MKDRSATGCR ALSDLRDLLG RAHVLTDGAT DPFARDWTGK WRADPLAVLR PATTQEVAEI
VRIAARHDLS VVPVGGNTGL VGGTANTGAL MVSLERMSAI REVRPEAGVM IVEAGAILSD
LHAAAAAHDL VFPLTFGARG SARVGGFLST NAGGSNVVRY GSTRGLVLGL EVVLADGRVL
DLMSELRKDN SGYDLRDLFI GAEGTLGLIT AAVLRLLPAP HHHATALAAI RDLPAALSLL
RRLQSATDGA VEAFEYMPRT YMRALAHHRP DLRQPFAIHD HTVMIDLGGL SRPLVDTLEE
VLSEAVEAGE VHDATIAQNE TQRARIWEMR EAAAEITFKR LPIVDNDVAL PLDGVAAFID
RMHERLAAID PAAETLIVAH LGDGNVHLTV YPDDGCRLED IREMVEDVTV GLGGSISAEH
GIGLSKLSTM TRRKDPVALD VMRAIKMALD PQDRMNPGKV VPKA
//
