ID A0A098UAA2_9BURK Unreviewed; 329 AA.
AC A0A098UAA2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:KGF81494.1};
GN ORFNames=IA69_12665 {ECO:0000313|EMBL:KGF81494.1};
OS Massilia sp. JS1662.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1519190 {ECO:0000313|EMBL:KGF81494.1, ECO:0000313|Proteomes:UP000029701};
RN [1] {ECO:0000313|EMBL:KGF81494.1, ECO:0000313|Proteomes:UP000029701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS1662 {ECO:0000313|EMBL:KGF81494.1,
RC ECO:0000313|Proteomes:UP000029701};
RA Fida T.T., Spain J.C.;
RT "Identification of Arachidin-3 degrading bacteria in the peanut
RT rhizosphere.";
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}.
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:KGF81494.1}.
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DR EMBL; JPQD01000011; KGF81494.1; -; Genomic_DNA.
DR RefSeq; WP_036233492.1; NZ_JPQD01000011.1.
DR AlphaFoldDB; A0A098UAA2; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000029701; 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 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; 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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 18..321
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..292
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 329 AA; 35401 MW; 33FC326B10A3CF5E CRC64;
MKIAILDDYQ DAVRGLECFR LLDGHEVKVF NNSTRGLGQL AIRLAPFDAL VLIRERTAFP
RALLAKLPNL KLISQTGKVS GHVDVAAATE HGIAIAEGVG SPVAPAELTW ALIMAASRKI
VPYANNLKDG LWQTASINPE LNGLGRVLKG RTLGIWGYGK IGHLIAGYAQ AFGMHVMVWG
SEKSRAAAVA DGLTAAPTRE AFFEQADVVS VHLRLNDATR GIVKADDLAR MKRDALFVNT
SRAELVEEGA LEAALRKGRP GYAALDVFTS EPLAGDAAIL KIPTVLATPH LGYVERDSYE
LYFRAAFENV VQFANGHPTN ILNPDALTG
//
