ID F4LRD2_TEPAE Unreviewed; 365 AA.
AC F4LRD2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Phosphoglycerate dehydrogenase {ECO:0000313|EMBL:CDI40955.1};
DE EC=1.1.1.95 {ECO:0000313|EMBL:CDI40955.1};
GN OrderedLocusNames=TEPIRE1_2308 {ECO:0000313|EMBL:CDI40955.1};
OS Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1).
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Tepidanaerobacteraceae; Tepidanaerobacter.
OX NCBI_TaxID=1209989 {ECO:0000313|EMBL:CDI40955.1, ECO:0000313|Proteomes:UP000010802};
RN [1] {ECO:0000313|Proteomes:UP000010802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Re1 {ECO:0000313|Proteomes:UP000010802};
RX PubMed=23469343; DOI=10.1128/genomeA.00213-12;
RA Manzoor S., Bongcam-Rudloff E., Schnurer A., Muller B.;
RT "First genome sequence of a syntrophic acetate-oxidizing bacterium,
RT Tepidanaerobacter acetatoxydans strain Re1.";
RL Genome Announc. 1:E00213-E00213(2013).
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; HF563609; CDI40955.1; -; Genomic_DNA.
DR RefSeq; WP_013779188.1; NC_019954.2.
DR AlphaFoldDB; F4LRD2; -.
DR STRING; 1209989.TepRe1_2145; -.
DR KEGG; tae:TepiRe1_2308; -.
DR KEGG; tep:TepRe1_2145; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_3_9; -.
DR Proteomes; UP000010802; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR CDD; cd12171; 2-Hacid_dh_10; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000010802}.
FT DOMAIN 68..347
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 137..315
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 365 AA; 41273 MW; 33D7DC0187D6AB4A CRC64;
MPSKKMKALL VGDAMIPVEG FEKATRKYLS DYVEEIYAYN WEENWDRLQE RRLIVEKNGP
EVEDVLPFIE KAIDAEMLLG LFVPVSKRNM DLMPNLKIVG VARAGLENVN VKEATRRGII
VFNVRGRNAE AVSDFAVGLM IAECRNIARA HHAIKNGIWR KEFSNSDWTP ELNGKTVGLV
GFGYIGKLVA KKLSGFGVNI IIYDPFVKKE KVEELGFRHV DKDTLFRESD FISLHARLSK
DTKNLVSEKE LSLMKPTAYL INTARAGLID QEALTNALKN KKIAGAGLDV FWEEPLPENS
EFLELDNVTL TTHIAGTTKE ALTRSPELLV RDIEKFLSEG KADFIINPEV LEKENVKKWL
KELKV
//
