ID M4RFB0_9BIFI Unreviewed; 409 AA.
AC M4RFB0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:AGH40869.1};
GN ORFNames=D805_0602 {ECO:0000313|EMBL:AGH40869.1};
OS Bifidobacterium thermophilum RBL67.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1254439 {ECO:0000313|EMBL:AGH40869.1, ECO:0000313|Proteomes:UP000011835};
RN [1] {ECO:0000313|EMBL:AGH40869.1, ECO:0000313|Proteomes:UP000011835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RBL67 {ECO:0000313|EMBL:AGH40869.1,
RC ECO:0000313|Proteomes:UP000011835};
RX PubMed=23640377;
RA Jans C., Lacroix C., Follador R., Stevens M.J.;
RT "Complete Genome Sequence of the Probiotic Bifidobacterium thermophilum
RT Strain RBL67.";
RL Genome Announc. 1:E00191-13(2013).
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; CP004346; AGH40869.1; -; Genomic_DNA.
DR RefSeq; WP_015450130.1; NC_020546.1.
DR AlphaFoldDB; M4RFB0; -.
DR KEGG; btp:D805_0602; -.
DR PATRIC; fig|1254439.12.peg.605; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_9_2_11; -.
DR Proteomes; UP000011835; 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; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 5..311
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 110..284
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 409 AA; 44423 MW; C663E6A5BFF2071A CRC64;
MPKALLLENI HPFAAQSLRD HGFEVETLKG ALSEDELIDA LEGVDLLGIR SKTNVTRKVI
DARPNLTAIG CFCIGTNQVD LDYAGKRGIA VFNAPYSNTR SVVELVICDI ICLMRRIPAH
THHMKHGVWD KSASGSHEVR GKTLGIIGYG NIGSQLSVLA EAMGMRVLFY DLEEKLAMGN
AKRMSSLNEL LEQSDAVTLH VDGRKSNTGF FGEEQFSHMK QGAIFINLSR GFVADLDALK
RHLDSGHISG AAVDVFPVEP KKSGDAFTTP LADEDNMILT PHIGGSTLEA QESIGHFVSQ
RLEDYWFKGS AALSVNFPQL NLGNNRGVAR IAHLHANLPG VLGKMNHILG EENINISAQS
LGTEGELGYV VTDVAEVPDQ ATIDALSHIE GTIRMRVLTD GNTVEDTEH
//
