ID A0A0G3X8S1_9SPHN Unreviewed; 312 AA.
AC A0A0G3X8S1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative dehydrogenase {ECO:0000313|EMBL:AKM07557.1};
GN ORFNames=AM2010_1487 {ECO:0000313|EMBL:AKM07557.1};
OS Pelagerythrobacter marensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Pelagerythrobacter.
OX NCBI_TaxID=543877 {ECO:0000313|EMBL:AKM07557.1, ECO:0000313|Proteomes:UP000037643};
RN [1] {ECO:0000313|EMBL:AKM07557.1, ECO:0000313|Proteomes:UP000037643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 22370 {ECO:0000313|EMBL:AKM07557.1,
RC ECO:0000313|Proteomes:UP000037643};
RA Kim K.M.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP011805; AKM07557.1; -; Genomic_DNA.
DR RefSeq; WP_047806545.1; NZ_LMVG01000005.1.
DR AlphaFoldDB; A0A0G3X8S1; -.
DR STRING; 543877.AM2010_1487; -.
DR KEGG; amx:AM2010_1487; -.
DR PATRIC; fig|543877.4.peg.1513; -.
DR OrthoDB; 9787219at2; -.
DR Proteomes; UP000037643; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd05300; 2-Hacid_dh_1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000037643}.
FT DOMAIN 31..302
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 105..274
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 312 AA; 34272 MW; 53E7E954875F6B6A CRC64;
MTVAVLSGLV RPLVEEHLPA GIEPRWYTSV EELHALAPEA EIGWFDLDAT EPMAEAVRRA
EKLRWLSSIY AGLDFLPLDL LQRRGVTITN GAGINAITIA EYVVMGMLTM AKGYREVVRA
QDRREWLADS PGKRELAGSR ALLLGYGAIG KLIRPRLEAF GVEVTVVRRS GGDGVLAPDE
WRARLGEFDW VILAVPATPE TDAMIGSEEL AAMKDDAVLV NIARGAVVDQ DALVAALEER
RIGGAFLDVT TPEPLPADHP LWQLENAHVT MHLSGRAQSK MFVRSAERFL ANCRRFVAGE
PLEPIFDPAR GY
//
