ID K6X4D6_9ALTE Unreviewed; 369 AA.
AC K6X4D6;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Oxidoreductase, FAD-binding family protein {ECO:0000313|EMBL:GAC15484.1};
GN ORFNames=GLIP_2863 {ECO:0000313|EMBL:GAC15484.1};
OS Aliiglaciecola lipolytica E3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Aliiglaciecola.
OX NCBI_TaxID=1127673 {ECO:0000313|EMBL:GAC15484.1, ECO:0000313|Proteomes:UP000006334};
RN [1] {ECO:0000313|EMBL:GAC15484.1, ECO:0000313|Proteomes:UP000006334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3 {ECO:0000313|EMBL:GAC15484.1,
RC ECO:0000313|Proteomes:UP000006334};
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=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the L2HGDH family.
CC {ECO:0000256|ARBA:ARBA00037941}.
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:GAC15484.1}.
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DR EMBL; BAEN01000056; GAC15484.1; -; Genomic_DNA.
DR RefSeq; WP_008845289.1; NZ_BAEN01000056.1.
DR AlphaFoldDB; K6X4D6; -.
DR STRING; 1127673.GLIP_2863; -.
DR eggNOG; COG0579; Bacteria.
DR OrthoDB; 9801699at2; -.
DR Proteomes; UP000006334; Unassembled WGS sequence.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProt.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR43104; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43104:SF4; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006334}.
FT DOMAIN 7..364
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 369 AA; 39601 MW; F8FD69073B0BF18B CRC64;
MVESVECVVI GAGVIGLAVA RQMALSNIET VVLEGQTQIG TGISSRNSEV IHAGIYYPPN
SLKAKLCVKG NKMLYSYCDD KNIHYQRCGK LIVATSDTQQ TKLQEIQRKA IANQVDDLQL
LSQQQVNALE PEIRCNAGLY SPSTGIIDSH GLMLNLQGDI ESAGGAIALG SPVVKATCQE
QGITLHVGGE QPCVLKAKFV INCAGLHAQP LAQRFAGVPV NTIPPLYYAK GSYFSLSGKS
PFSHLIYPLP ESAGLGVHST LDLGGGVKFG PDVEWVDRLD YRVDPTKSTE FYAKIREYWP
SLKDDSLHPA YAGIRPKLHP QGVTAHDFMI QTADTHGVKG LVNLYGFESP GLTASLAIGE
EVANVLLAS
//
