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Database: UniProt
Entry: A0A0P1F939_THAGE
LinkDB: A0A0P1F939_THAGE
Original site: A0A0P1F939_THAGE 
ID   A0A0P1F939_THAGE        Unreviewed;       531 AA.
AC   A0A0P1F939;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   22-NOV-2017, entry version 15.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|RuleBase:RU363003};
DE            EC=1.1.1.95 {ECO:0000256|RuleBase:RU363003};
GN   Name=serA {ECO:0000313|EMBL:CUH64655.1};
GN   ORFNames=TG4357_01415 {ECO:0000313|EMBL:CUH64655.1};
OS   Thalassobius gelatinovorus (Ruegeria gelatinovora).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Thalassobius.
OX   NCBI_TaxID=53501 {ECO:0000313|EMBL:CUH64655.1, ECO:0000313|Proteomes:UP000051587};
RN   [1] {ECO:0000313|EMBL:CUH64655.1, ECO:0000313|Proteomes:UP000051587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 4357 {ECO:0000313|EMBL:CUH64655.1,
RC   ECO:0000313|Proteomes:UP000051587};
RG   Swine Surveillance;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + NAD(+) = 3-
CC       phosphonooxypyruvate + NADH. {ECO:0000256|RuleBase:RU363003}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glycerate: step 1/3.
CC       {ECO:0000256|RuleBase:RU363003}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU363003}.
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DR   EMBL; CYSA01000015; CUH64655.1; -; Genomic_DNA.
DR   RefSeq; WP_058262152.1; NZ_FOFW01000002.1.
DR   EnsemblBacteria; CUH64655; CUH64655; TG4357_01415.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000051587; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1330.90; -; 1.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR029009; ASB_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   InterPro; IPR006236; PGDH.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   Pfam; PF01842; ACT; 1.
DR   SUPFAM; SSF143548; SSF143548; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01327; PGDH; 1.
DR   PROSITE; PS51671; ACT; 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   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU363003};
KW   Complete proteome {ECO:0000313|Proteomes:UP000051587};
KW   NAD {ECO:0000256|RuleBase:RU363003};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU363003,
KW   ECO:0000313|EMBL:CUH64655.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051587};
KW   Serine biosynthesis {ECO:0000256|RuleBase:RU363003}.
FT   DOMAIN      456    531       ACT. {ECO:0000259|PROSITE:PS51671}.
SQ   SEQUENCE   531 AA;  56695 MW;  46FC5C06FFDFE8C9 CRC64;
     MAPKVLVSDK LSETAVQIFR DRGIDVDFLP DVGKDKDKLA EIIGQYDGLA IRSATKVTPA
     ILEKADKLKV IGRAGIGTDN VDKEAASKKG VIVMNTPFGN MITTAEHAIA MMFAAARQLP
     EASASTHAGK WEKSKFMGVE LTNKTLGVIG AGNIGGIVCD RARGLKMKVI AYDPFLSQEK
     AEKMQVEKVE LDELLERADF ITLHVPLTDT TRNILSRENL AKTKKGVRVI NCARGGLVDE
     VALAEMLKSG HVAGAAFDVF SEEPAKENPL FNLPNVVCTP HLGAATTEAQ ENVALQVAEQ
     MANYLLDGAV ENALNMPSMT AEEAKVMGPW VALAGHLGSY IGQLTDEPIK AINILYDGVV
     SDMNLPALNC AVVAGIMKKV NPDVNMVSAP VVAKERGIQI STTNQDKSGA FDGYIKVTIV
     TPERERSIAG TVFSDGKPRF IQIKGINIDA EVGSHMLYTT NEDVPGIIGT LGRVLGDNGV
     NIANFTLGRA QAGGEAIALL YVDGEVDQKV LDELAATGLF KQIKPLSFDV A
//
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