ID   L2HDH_INDAL             Reviewed;         399 AA.
AC   S2DJ52;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=L-2-hydroxyglutarate dehydrogenase {ECO:0000305|PubMed:34555022};
DE            EC=1.1.99.2 {ECO:0000269|PubMed:34555022};
GN   ORFNames=A33Q_0852 {ECO:0000312|EMBL:EOZ98997.1};
OS   Indibacter alkaliphilus (strain CCUG 57479 / KCTC 22604 / LW1).
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cyclobacteriaceae.
OX   NCBI_TaxID=1189612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 57479 / KCTC 22604 / LW1;
RX   PubMed=23868132; DOI=10.1128/genomea.00513-13;
RA   Singh A., Kumar Jangir P., Sharma R., Singh A., Kumar Pinnaka A.,
RA   Shivaji S.;
RT   "Draft Genome Sequence of Indibacter alkaliphilus Strain LW1T, Isolated
RT   from Lonar Lake, a Haloalkaline Lake in the Buldana District of
RT   Maharashtra, India.";
RL   Genome Announc. 1:E00513-E00513(2013).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=34555022; DOI=10.1371/journal.pcbi.1009446;
RA   Rembeza E., Engqvist M.K.M.;
RT   "Experimental and computational investigation of enzyme functional
RT   annotations uncovers misannotation in the EC 1.1.3.15 enzyme class.";
RL   PLoS Comput. Biol. 17:e1009446-e1009446(2021).
CC   -!- FUNCTION: Catalyzes the dehydrogenation of L-2-hydroxyglutarate (L2HG
CC       or(S)-2-hydroxyglutarate) to 2-oxoglutarate (alpha-ketoglutarate).
CC       Active in vitro with the artificial electron acceptor 2,6-
CC       dichlorophenolindophenol (DCPIP). Also displays a very low oxidase
CC       activity in vitro on L-2-hydroxyglutarate with O2 as the electron
CC       acceptor, but this activity is most likely not physiological.
CC       {ECO:0000269|PubMed:34555022}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2;
CC         Xref=Rhea:RHEA:21252, ChEBI:CHEBI:13193, ChEBI:CHEBI:16782,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:17499; EC=1.1.99.2;
CC         Evidence={ECO:0000269|PubMed:34555022};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q9H9P8};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.22 mM for (S)-2-hydroxyglutarate (at pH 7.4 and 25 degrees
CC         Celsius) {ECO:0000269|PubMed:34555022};
CC         Note=kcat is 3.7 sec(-1) with DCPIP as electron acceptor (at pH 7.4
CC         and 25 degrees Celsius). {ECO:0000269|PubMed:34555022};
CC   -!- SIMILARITY: Belongs to the L2HGDH family. {ECO:0000305}.
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DR   EMBL; ALWO02000020; EOZ98997.1; -; Genomic_DNA.
DR   RefSeq; WP_009036253.1; NZ_ALWO02000020.1.
DR   STRING; 1189612.A33Q_0852; -.
DR   EnsemblBacteria; EOZ98997; EOZ98997; A33Q_0852.
DR   eggNOG; COG0579; Bacteria.
DR   OrthoDB; 1371190at2; -.
DR   Proteomes; UP000006073; Unassembled WGS sequence.
DR   GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047545; F:2-hydroxyglutarate dehydrogenase activity; IEA:RHEA.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..399
FT                   /note="L-2-hydroxyglutarate dehydrogenase"
FT                   /id="PRO_0000454862"
SQ   SEQUENCE   399 AA;  44131 MW;  6CD0B04533D81805 CRC64;
     MDFQVIIIGG GIVGLATGLK IKQRNPNIKV ALLEKEEEVA KHQTGNNSGV IHSGLYYKPG
     SLKAKNCIEG YHELVRFCEE ENIPFELTGK VVVATRKEQV PLLNSLLERG LQNGLKGTRS
     ITLDELKHFE PYCAGVAAIH VPQTGIVDYK LVAEKYAEKF QILGGQVFLG HKVIKVETQN
     TASIIHTSKG SFSTNLLINC AGLYSDKVAQ MNQKESLDVK IIPFRGEYYK IKKEREYLVK
     NLIYPVPDPN FPFLGVHFTR MMKGGVEAGP NAVLAFKREG YKKSQVNFSE LAETLSWPGF
     QKVASKYWKT GMGELFRSFS KKAFTDALKE LIPDIQESDL IEGGAGVRAQ ACDRTGGLLD
     DFCIREDQNA IHVLNAPSPA ATSSLSIGGT VCEWALKRF