ID A0A1M6F2J6_9CLOT Unreviewed; 317 AA.
AC A0A1M6F2J6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:SHI91938.1};
GN ORFNames=SAMN05444401_1787 {ECO:0000313|EMBL:SHI91938.1};
OS Clostridium amylolyticum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121298 {ECO:0000313|EMBL:SHI91938.1, ECO:0000313|Proteomes:UP000184080};
RN [1] {ECO:0000313|EMBL:SHI91938.1, ECO:0000313|Proteomes:UP000184080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21864 {ECO:0000313|EMBL:SHI91938.1,
RC ECO:0000313|Proteomes:UP000184080};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQZO01000002; SHI91938.1; -; Genomic_DNA.
DR RefSeq; WP_073005636.1; NZ_FQZO01000002.1.
DR AlphaFoldDB; A0A1M6F2J6; -.
DR STRING; 1121298.SAMN05444401_1787; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000184080; 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; cd12161; GDH_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; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000184080}.
FT DOMAIN 21..311
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 112..286
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 317 AA; 34577 MW; 5772BCD41BF7698E CRC64;
MNIVLLEPLA VSEEVLNKLS LTLTEAGHNF KHYDSVEKDI NVLKERVKDA DILIIANNPL
KGEVIRAAKN LKYISVAFTG VDHVDKEACM ERGIKVSNAA GYSTDSVAEL TLGMIIAALR
NVLPCDERTR NLGTKDGLVG FELKGKTVGI VGTGAIGLRV AEILKVFNCK LLGYSRTEKQ
EGKNLGIKYV SLEELLRKSD IVTLHTPLNA ETKHLINKER IAMMKKSSIL INAARGAVVD
SAALAEALNQ GIIGAAAIDV FENEPPIEKN HPLLNAKNTI VTPHIAFATK ESMVYRAEIT
FDNVYAYLKG EGKNIVF
//
