ID A0A101J6D1_9ACTN Unreviewed; 325 AA.
AC A0A101J6D1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Phosphoglycerate dehydrogenase {ECO:0000313|EMBL:KUL21079.1};
GN ORFNames=ADL12_45395 {ECO:0000313|EMBL:KUL21079.1};
OS Streptomyces regalis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68262 {ECO:0000313|EMBL:KUL21079.1, ECO:0000313|Proteomes:UP000053923};
RN [1] {ECO:0000313|Proteomes:UP000053923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3151 {ECO:0000313|Proteomes:UP000053923};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUL21079.1}.
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DR EMBL; LLZG01000411; KUL21079.1; -; Genomic_DNA.
DR RefSeq; WP_062714605.1; NZ_LLZG01000411.1.
DR AlphaFoldDB; A0A101J6D1; -.
DR OrthoDB; 117809at2; -.
DR Proteomes; UP000053923; Unassembled WGS sequence.
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 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; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000053923}.
FT DOMAIN 43..325
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 114..293
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 325 AA; 34030 MW; A5E8A8DC154D0086 CRC64;
MTAPKNVLAV ISPHVGGRDI GAGLATLFPE GANVTVVEVA DEDPAALRAA HVVITALAPV
TAEHLAAAPE LELVQCASHG FDYVDVDAAR ERGVRVCNIG SSGAEAQNVA EQTFALMLAL
AKQIVPAHTA LVEADWALPR LQHSLTELSG KTLGIVGLGQ IGRQVARRAA AFDMSVVYAG
RRRLPPEKEA EFGGARHVPL DELLRTADYV SLHAPLTDET RDLLNAERLA LLKPTAFVIN
TARGALIDQD ALADALEKGA LAGAGIDVFD PEPPTAALRL LRAPNVVLSP HVSGVTRETL
VRIALAAVEN VTAFLSGGAP RDVVN
//
