ID K2HPC7_9RHOB Unreviewed; 394 AA.
AC K2HPC7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:EKE44719.1};
GN ORFNames=OCGS_1102 {ECO:0000313|EMBL:EKE44719.1};
OS Oceaniovalibus guishaninsula JLT2003.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Oceaniovalibus.
OX NCBI_TaxID=1231392 {ECO:0000313|EMBL:EKE44719.1, ECO:0000313|Proteomes:UP000006765};
RN [1] {ECO:0000313|EMBL:EKE44719.1, ECO:0000313|Proteomes:UP000006765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLT2003 {ECO:0000313|EMBL:EKE44719.1,
RC ECO:0000313|Proteomes:UP000006765};
RX PubMed=23144420; DOI=10.1128/JB.01874-12;
RA Tang K., Liu K., Jiao N.;
RT "Draft Genome Sequence of Oceaniovalibus guishaninsula JLT2003T.";
RL J. Bacteriol. 194:6683-6683(2012).
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}.
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:EKE44719.1}.
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DR EMBL; AMGO01000020; EKE44719.1; -; Genomic_DNA.
DR AlphaFoldDB; K2HPC7; -.
DR STRING; 1231392.OCGS_1102; -.
DR PATRIC; fig|1231392.3.peg.1107; -.
DR eggNOG; COG0277; Bacteria.
DR Proteomes; UP000006765; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000006765}.
FT DOMAIN 33..211
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 394 AA; 42082 MW; 49821D8741498EAF CRC64;
MDIFERLRAI LGDAHVRTGA DMAGFDRDWT GRYAFTPLAV LRPADTQQVA AIMRLAHETR
VPVVPFGGNT GLMGGTVAEG ALAISLERMN RIRDIRPAAR IAVVEAGVVL SQLHDAAEAQ
GLVFPLTFGA RQSARIGGVL GTNAGGSNVV RYGNTRALCL GLEVVLPDGR ILDMMSQLMK
DNSGYDLRDL FIGAEGTLGI VTAAVLRLAP RPLAYATAMV AVPSLDDALA LLNALQEGTG
GAVEAFEYMP RDYIDAHLAH DPKARRPFDA DHDHTIMVEV GATAARDAMP GPDGAVPVVA
RLEEMLAAMI KEGRVLDANV ARSEAQRREI WARREAAGEL TVAGGPGIIT DVSVPLDRVA
EFLRRAYADV TARDPQARFM TVSHLGDGNV HLTI
//
