ID E7AAA2_HELFC Unreviewed; 400 AA.
AC E7AAA2;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=L-2-hydroxyglutarate oxidase, FAD dependent oxidoreductase {ECO:0000313|EMBL:CBY83475.1};
GN OrderedLocusNames=Hfelis_13910 {ECO:0000313|EMBL:CBY83475.1};
OS Helicobacter felis (strain ATCC 49179 / NCTC 12436 / CS1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=936155 {ECO:0000313|EMBL:CBY83475.1, ECO:0000313|Proteomes:UP000007934};
RN [1] {ECO:0000313|Proteomes:UP000007934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49179 / NCTC 12436 / CS1
RC {ECO:0000313|Proteomes:UP000007934};
RA Arnold A., Zigova Z., Lawley T., Falkow S., Bentley S., Aslett M.,
RA Muller A.;
RT "Comparative whole genome analysis of the carcinogenic bacterial pathogen
RT Helicobacter felis.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBY83475.1, ECO:0000313|Proteomes:UP000007934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49179 / NCTC 12436 / CS1
RC {ECO:0000313|Proteomes:UP000007934};
RX PubMed=21402865;
RA Arnold I.C., Zigova Z., Holden M., Lawley T.D., Rad R., Dougan G.,
RA Falkow S., Bentley S.D., Muller A.;
RT "Comparative whole genome sequence analysis of the carcinogenic bacterial
RT model pathogen Helicobacter felis.";
RL Genome Biol. Evol. 3:302-308(2011).
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; FQ670179; CBY83475.1; -; Genomic_DNA.
DR RefSeq; WP_013469839.1; NC_014810.2.
DR AlphaFoldDB; E7AAA2; -.
DR STRING; 936155.HFELIS_13910; -.
DR GeneID; 36134666; -.
DR KEGG; hfe:HFELIS_13910; -.
DR eggNOG; COG0579; Bacteria.
DR HOGENOM; CLU_024775_0_1_7; -.
DR OrthoDB; 9801699at2; -.
DR Proteomes; UP000007934; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007934}.
FT DOMAIN 6..393
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 400 AA; 44529 MW; 60C53B0CC1873B35 CRC64;
MAVIYDFIII GGGILGHSVA MQLLDKYPDA KIALLEKEPS SALHQTGRNS GVIHAGVYYT
PGTLKANFCY EGNRATKAFC EDNGIVYEQC GKLLVASNAL ELQRMENLWE RTKENGLERV
RLNAQELQEM EKNIVGLGGI FFPTSAIVSY VEVTRAMAKR FQEKGGEIFY NTQVVALSEH
ARGVKILSKN GVFETNYLIT CCGLHSDRIV KMLGIMPKFT ICPFRGEYFK LAGHCNKIVK
HLIYPIPDPQ VPFLGVHLTR MIDGSVTVGP NAVLAFKREG YAKSDVSWGD LKEMLIHKGV
RQVIKTHFKT GCSEFRHSFC KKSYLSLVQK YCPSLKLEDL RAHPAGVRAQ AVSENGELIE
DFLFCNTERS VNVCNAPSPA ATSALPIGRH ILERLENILK
//
