ID K2KJ35_9PROT Unreviewed; 477 AA.
AC K2KJ35;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Putative FAD-binding dehydrogenase {ECO:0000313|EMBL:EKE77295.1};
GN ORFNames=P24_05922 {ECO:0000313|EMBL:EKE77295.1};
OS Oceanibaculum indicum P24.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Oceanibaculaceae; Oceanibaculum.
OX NCBI_TaxID=1207063 {ECO:0000313|EMBL:EKE77295.1, ECO:0000313|Proteomes:UP000006746};
RN [1] {ECO:0000313|EMBL:EKE77295.1, ECO:0000313|Proteomes:UP000006746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P24 {ECO:0000313|EMBL:EKE77295.1,
RC ECO:0000313|Proteomes:UP000006746};
RX PubMed=23209207; DOI=10.1128/JB.01859-12;
RA Lai Q., Shao Z.;
RT "Genome Sequence of Oceanibaculum indicum Type Strain P24.";
RL J. Bacteriol. 194:6942-6942(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:EKE77295.1}.
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DR EMBL; AMRL01000005; EKE77295.1; -; Genomic_DNA.
DR RefSeq; WP_008943796.1; NZ_AMRL01000005.1.
DR AlphaFoldDB; K2KJ35; -.
DR STRING; 1207063.P24_05922; -.
DR PATRIC; fig|1207063.3.peg.1198; -.
DR eggNOG; COG0277; Bacteria.
DR Proteomes; UP000006746; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000006746}.
FT DOMAIN 43..224
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 477 AA; 51677 MW; 0898E26874BD8925 CRC64;
MKALAETVID DTLQRIRALV GDKGYITAAD AMEPHLVEWR GLWRGQARAV VKPADTAEVA
EVVKLCAEAG IPIVPQGGNT SLVGGSVPYE DFDGIILSLA RMNRVRAIDR MNYTMTVEAG
CVLADLQRIA EENDRFFPLS LAAEGSCMIG GNLSTNAGGV NVLRYGNTRE LVLGLEVALP
DGTVWEGLRG LRKDNTGYDL KHLFVGAEGT LGIVTAAVLK LFPKPTRRET AMVAISGPDA
AIELLARARA ASADGVTSFE LMPRICFDFV LAHIADTVDP LPQRYDWHVL LELSSTSPED
DGLAEKLQNL LEKAAEDGLV LDAAIAQNQA QANAMWKLRE TVSEAQKPEG ASIKHDVSVP
VSRVPEFLRR ADEAVAKAVP GIRVVGFGHV GDGNIHYNLS VPKGGDNQAF LARWEEINEI
VHDIVHDMGG SISAEHGLGR LKREEITRYK SQTEMELMRK IKGLIDPKGI MNPGKVL
//
