ID Q4KDZ4_PSEF5 Unreviewed; 397 AA.
AC Q4KDZ4;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=L-2-hydroxyglutarate oxidase {ECO:0000313|EMBL:AAY91705.1};
GN Name=lhgO {ECO:0000313|EMBL:AAY91705.1};
GN OrderedLocusNames=PFL_2432 {ECO:0000313|EMBL:AAY91705.1};
OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664 {ECO:0000313|EMBL:AAY91705.1, ECO:0000313|Proteomes:UP000008540};
RN [1] {ECO:0000313|EMBL:AAY91705.1, ECO:0000313|Proteomes:UP000008540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5
RC {ECO:0000313|Proteomes:UP000008540};
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S.III.,
RA Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000076; AAY91705.1; -; Genomic_DNA.
DR RefSeq; WP_011060730.1; NC_004129.6.
DR AlphaFoldDB; Q4KDZ4; -.
DR STRING; 220664.PFL_2432; -.
DR GeneID; 57475486; -.
DR KEGG; pfl:PFL_2432; -.
DR PATRIC; fig|220664.5.peg.2475; -.
DR eggNOG; COG0579; Bacteria.
DR HOGENOM; CLU_024775_0_1_6; -.
DR Proteomes; UP000008540; Chromosome.
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:SF2; 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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 4..392
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 397 AA; 43540 MW; 3EAC5FA564C80709 CRC64;
MIYDFCIIGG GIVGLATAME ILKRQPGASL VILEKENVLA KHQTGHNSGV IHAGIYYAPG
SLKADLCKRG AEATKQFCSE HGIKFEVCGK VLVASNALEV QRMEALYQRS QQNGLKVERL
DAEQLRQREP NIVGLGGLFL DATGIVDYRE VCDTMARVIR REGGEICLSQ TVTAIQESAD
SVTVSSHGGS WRAKKLVACA GLQSDRLAVM AGVKIDHQII PFRGEYFRLP ASKNNIVNHL
IYPIPDPELP FLGVHLTRMI DGSVTVGPNA VLGLGRENYR KFSINWRDVA QYASFPGFWK
TIWQNLGSGT TEMKNSLFKS GYLEQCRKYC PSLQVEDLLP YEAGIRAQAV MRDGSLVHDF
LFAETPRMLH VCNAPSPAAT SAIPIGSMIA DRIFQAA
//
