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Database: UniProt
Entry: A0A0M2UWZ8_9BACT
LinkDB: A0A0M2UWZ8_9BACT
Original site: A0A0M2UWZ8_9BACT 
ID   A0A0M2UWZ8_9BACT        Unreviewed;       526 AA.
AC   A0A0M2UWZ8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, 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   ORFNames=BROFUL_00707 {ECO:0000313|EMBL:KKO20588.1};
OS   Candidatus Brocadia fulgida.
OC   Bacteria; Planctomycetes; Planctomycetia; Candidatus Brocadiales;
OC   Candidatus Brocadiaceae; Candidatus Brocadia.
OX   NCBI_TaxID=380242 {ECO:0000313|EMBL:KKO20588.1, ECO:0000313|Proteomes:UP000034954};
RN   [1] {ECO:0000313|EMBL:KKO20588.1, ECO:0000313|Proteomes:UP000034954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RU1 {ECO:0000313|EMBL:KKO20588.1};
RX   PubMed=24267221; DOI=10.1186/1471-2180-13-265;
RA   Ferousi C., Speth D.R., Reimann J., Op den Camp H.J., Allen J.W.,
RA   Keltjens J.T., Jetten M.S.;
RT   "Identification of the type II cytochrome c maturation pathway in
RT   anammox bacteria by comparative genomics.";
RL   BMC Microbiol. 13:265-265(2013).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KKO20588.1}.
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DR   EMBL; LAQJ01000089; KKO20588.1; -; Genomic_DNA.
DR   PATRIC; fig|380242.3.peg.899; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000034954; 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; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU363003};
KW   Complete proteome {ECO:0000313|Proteomes:UP000034954};
KW   NAD {ECO:0000256|RuleBase:RU363003};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU363003};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034954};
KW   Serine biosynthesis {ECO:0000256|RuleBase:RU363003}.
FT   DOMAIN      454    526       ACT. {ECO:0000259|PROSITE:PS51671}.
SQ   SEQUENCE   526 AA;  56175 MW;  B6F1135093F6BC5E CRC64;
     MQVLIADELP DICIEILEKA GLTVVNKPGV KADELKAIIA SCDGIILRSG TKITASLLEG
     ADRLKAVCRA GVGVDNVDVP AATKKGIVVM NTPEGNIIST AEHTVALLFS LSRFVPQACA
     SVKAGKWERK KFTGIQITGK TLGIIGLGRV GRQVAKRAAA LEMKVVGYDP FISPEVTAQY
     SIQIAKNLKE LLSQADYITI HVPFNSETKN LITRNEFPIM KPGVRIINCA RGGIISEEDL
     YQAIKNGQVA GAAIDVFDVE PPVGNKLLEL DQVITTPHLG ASTEEAQVAV AIEAAEQMAD
     ALTGKGFRNA VNLPPYNIEE YNALKPYILL AERMGLLLSQ LAVGGISEVD IIYTGEITKK
     NICLVTDSLM VGLLKPALED GVNLVSAPHL IAERGIKTNI TTSSGASDFT SLLTAKITTS
     QGKTAISGTV FGKNEPRIVD INGYGVEAVI DKYMLVLFGK DKPGLIGNIG RVLGNKDINI
     AHMTFGRKET GGNAITIVNV DAQIPKECLL EIGKIDHIEA AYLVRF
//
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