ID C7JH84_ACEP3 Unreviewed; 419 AA.
AC C7JH84;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:BAH99338.1};
GN OrderedLocusNames=APA01_11910 {ECO:0000313|EMBL:BAH99338.1};
OS Acetobacter pasteurianus (strain NBRC 105184 / IFO 3283-01).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=634452 {ECO:0000313|EMBL:BAH99338.1, ECO:0000313|Proteomes:UP000000948};
RN [1] {ECO:0000313|EMBL:BAH99338.1, ECO:0000313|Proteomes:UP000000948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105184 / IFO 3283-01 {ECO:0000313|Proteomes:UP000000948};
RX PubMed=19638423; DOI=10.1093/nar/gkp612;
RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., Harada T.,
RA Hirakawa H., Kuhara S., Matsushita K., Fujita N., Shirai M.;
RT "Whole-genome analyses reveal genetic instability of Acetobacter
RT pasteurianus.";
RL Nucleic Acids Res. 37:5768-5783(2009).
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; AP011121; BAH99338.1; -; Genomic_DNA.
DR RefSeq; WP_004449129.1; NC_013209.1.
DR AlphaFoldDB; C7JH84; -.
DR STRING; 634452.APA01_11910; -.
DR GeneID; 66350049; -.
DR KEGG; apt:APA01_11910; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_9_2_5; -.
DR BioCyc; APAS634452:APA01_RS06020-MONOMER; -.
DR Proteomes; UP000000948; 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; cd04901; ACT_3PGDH; 1.
DR CDD; cd12176; PGDH_3; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR029752; D-isomer_DH_CS1.
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; SSF55021; ACT-like; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 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}.
FT DOMAIN 16..324
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 122..297
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 419 AA; 45491 MW; 7ACF1F93D61C1D6A CRC64;
MSTSTHLSLP KDKIRILLLE GIHDSAVALL KASGYENVVR HKGALEGDAL KEALEGVHIV
GIRSRTQLTK EVLDGADRLM AIGCFCIGTN QVDLEAARMN GIPVFNAPYS NTRSVAELVM
GEIVMLMRRI FPRSVECHEG KWSKSAHNSW EVRGKTLGIV GYGSIGSQLS VLAEAFGMRV
VYYDVVDKLG HGNALPVETL EDLLAQSDVV SLHVPQLPTT KNLMGEAQIK AMKKGSFLIN
NARGNVVDLD ALAEALKSGH LLGAAIDVYP KEPKGPNDKL ETPVQGLDNV ILSPHVGGST
VEAQERIGVE VARKLVEYSD VGSTFGSVNF PGVQLPQSPR GTRFMHAHRN VPGMMMRLNE
IFMNADCNVT AQFLQTDGEI GYVVIEADTG GNTELDDRLL QDLRGMEGTI RARLIYKGK
//
