ID F5YKG6_TREPZ Unreviewed; 324 AA.
AC F5YKG6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Phosphoglycerate dehydrogenase {ECO:0000313|EMBL:AEF84287.1};
DE EC=1.1.1.95 {ECO:0000313|EMBL:AEF84287.1};
GN OrderedLocusNames=TREPR_1968 {ECO:0000313|EMBL:AEF84287.1};
OS Treponema primitia (strain ATCC BAA-887 / DSM 12427 / ZAS-2).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=545694 {ECO:0000313|EMBL:AEF84287.1, ECO:0000313|Proteomes:UP000009223};
RN [1] {ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RA Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A.,
RA Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., Lucey K.,
RA Ballor N.R., Ottesen E., Rosenthal R., Allen A., Leadbetter J.R.,
RA Paulsen I.T.;
RT "Complete sequence of Treponema primitia strain ZAS-2.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEF84287.1, ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RX PubMed=21326336; DOI=10.1038/ismej.2011.3;
RA Rosenthal A.Z., Matson E.G., Eldar A., Leadbetter J.R.;
RT "RNA-seq reveals cooperative metabolic interactions between two termite-gut
RT spirochete species in co-culture.";
RL ISME J. 5:1133-1142(2011).
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; CP001843; AEF84287.1; -; Genomic_DNA.
DR RefSeq; WP_015708185.1; NC_015578.1.
DR AlphaFoldDB; F5YKG6; -.
DR STRING; 545694.TREPR_1968; -.
DR KEGG; tpi:TREPR_1968; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_3_12; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000009223; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR CDD; cd12173; PGDH_4; 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:UP000009223}.
FT DOMAIN 4..311
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 105..279
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT REGION 305..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 324 AA; 35687 MW; 255558C23773BF47 CRC64;
MYKVLIPEDV DSSGKDYLLE RGYEIKVGVP TDIETLKREI ADADALLARI ARFPEEVLAA
GKKLKVIARH GVGVDTVAVD YAESQGIWVV NAPLSNGNTV AECAVAMIMA LECDLIRLDR
KTREGDWTYR EHLKRRDLAG LTLGIVGFGR IGRMVAEKVS GLGMKILTYH PRKHPETPLM
VEHTTDFSRI LSSSDYLGVF VPSTSETRGM FNYAAFSAMK PSAYYINCAR GDTYVEADLA
RALDEGRLAG AAVDVFDPEP RFDSPLYRMD QVIVTQHSAG LSVEANYKMS LDAAKGIDEI
LRGDKPTWPV NHPAHPRADS TVSP
//
