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Database: UniProt
Entry: E7G2C8_9HELI
LinkDB: E7G2C8_9HELI
Original site: E7G2C8_9HELI 
ID   E7G2C8_9HELI            Unreviewed;       228 AA.
AC   E7G2C8;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:EFX42426.1};
GN   Name=serA {ECO:0000313|EMBL:EFX42426.1};
GN   ORFNames=HSUHS5_0058 {ECO:0000313|EMBL:EFX42426.1};
OS   Helicobacter suis HS5.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=710394 {ECO:0000313|EMBL:EFX42426.1, ECO:0000313|Proteomes:UP000054093};
RN   [1] {ECO:0000313|EMBL:EFX42426.1, ECO:0000313|Proteomes:UP000054093}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS5 {ECO:0000313|EMBL:EFX42426.1,
RC   ECO:0000313|Proteomes:UP000054093};
RX   PubMed=21414191; DOI=10.1186/1297-9716-42-51;
RA   Vermoote M., Vandekerckhove T.T., Flahou B., Pasmans F., Smet A.,
RA   De Groote D., Van Criekinge W., Ducatelle R., Haesebrouck F.;
RT   "Genome sequence of Helicobacter suis supports its role in gastric
RT   pathology.";
RL   Vet. Res. 42:51-51(2011).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC       ECO:0000256|RuleBase:RU003719}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFX42426.1}.
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DR   EMBL; ADHO01000012; EFX42426.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7G2C8; -.
DR   Proteomes; UP000054093; Unassembled WGS sequence.
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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR   PANTHER; PTHR42938:SF9; FORMATE DEHYDROGENASE 1; 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.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054093}.
FT   DOMAIN          3..105
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          106..224
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   228 AA;  25307 MW;  F3825F16992E0FED CRC64;
     MHIAICDPIH PKGLKLLQEQ RDFTFVDYSN LPKDELPLAI KDAHVLITRS MTAINASMLK
     EAHTLKAVVR AGVGVDNVDI QYCSQRGIVV MNVPTANTIA AVELTMAHLL NAVRCFPGAN
     AQLKLKRLWK REDWYGTELF GKKLGIIGFG NIGSRVGVRA LAFGMEVYTY DPYISKSKAT
     DLGVIYTKNF NDILACDIIT IHTPKNQETI NIIDTEQIAQ MKEGGDFN
//
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