ID A0A076MZB3_AMYME Unreviewed; 316 AA.
AC A0A076MZB3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Phosphoglycerate dehydrogenase-like oxidoreductase {ECO:0000313|EMBL:AIJ24266.1};
GN Name=serA {ECO:0000313|EMBL:AIJ24266.1};
GN ORFNames=AMETH_4174 {ECO:0000313|EMBL:AIJ24266.1};
OS Amycolatopsis methanolica 239.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis; Amycolatopsis methanolica group.
OX NCBI_TaxID=1068978 {ECO:0000313|EMBL:AIJ24266.1, ECO:0000313|Proteomes:UP000062973};
RN [1] {ECO:0000313|EMBL:AIJ24266.1, ECO:0000313|Proteomes:UP000062973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=239 {ECO:0000313|EMBL:AIJ24266.1,
RC ECO:0000313|Proteomes:UP000062973};
RA Tang B.;
RT "Whole Genome Sequence of the Amycolatopsis methanolica 239.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP009110; AIJ24266.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A076MZB3; -.
DR STRING; 1068978.AMETH_4174; -.
DR KEGG; amq:AMETH_4174; -.
DR PATRIC; fig|1068978.7.peg.4471; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_3_11; -.
DR Proteomes; UP000062973; 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; cd12169; PGDH_like_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; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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:UP000062973}.
FT DOMAIN 22..311
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 113..284
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 316 AA; 34711 MW; 6239D0D470FEB316 CRC64;
MNTMKIVVLD DYQDVARSLA DWDSLGAEVE VITSYVGDHD ELVRRLAGAE VVVAMRERTR
FTAEVLERLP DLKLLVSTGR RNAAIDLKAT ERLGITVCGT GYLPHPTAEH TWALILAAQR
HLETELAAMR DGAWQSTVGI GLHDKTLGLL GLGNLGQQVA RIGQAFGMET IAWSQNLTAE
RAAEHGVTAV SKEDLFARAD VLSVHLVLSK RTRGLVGAAE LAAMKPGALL VNTSRGPIID
EQALLDALRE RRIRAALDVY DIEPLPADHP LRAMRNATLT PHLGYVTREV YEIFYRDAVE
DIAAWRDGNP VRVMTL
//
