ID A0A0K2X9Y2_9HELI Unreviewed; 314 AA.
AC A0A0K2X9Y2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:CRF42876.1};
DE EC=1.1.1.95 {ECO:0000313|EMBL:CRF42876.1};
GN ORFNames=HAL011_06060 {ECO:0000313|EMBL:CRF40837.1}, HAL013_10870
GN {ECO:0000313|EMBL:CRF42876.1}, HAL07_06360
GN {ECO:0000313|EMBL:CRI32161.1}, HAL09_06270
GN {ECO:0000313|EMBL:CRF44058.1};
OS Helicobacter ailurogastricus.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1578720 {ECO:0000313|EMBL:CRF42876.1, ECO:0000313|Proteomes:UP000045175};
RN [1] {ECO:0000313|EMBL:CRF42876.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASB11 {ECO:0000313|EMBL:CRF40837.1}, ASB13
RC {ECO:0000313|EMBL:CRF42876.1}, ASB7 {ECO:0000313|EMBL:CRI32161.1}, and
RC ASB9 {ECO:0000313|EMBL:CRF44058.1};
RA Misic A.M., Cain C., Morris D.O., Rankin S., Beiting D.;
RT "Whole genome sequences of four Staphylococcus schleiferi canine
RT isolates.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000038622, ECO:0000313|Proteomes:UP000041394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jaenicke S.;
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CDML01000018; CRF40837.1; -; Genomic_DNA.
DR EMBL; CDMH01000048; CRF42876.1; -; Genomic_DNA.
DR EMBL; CDMN01000025; CRF44058.1; -; Genomic_DNA.
DR EMBL; CDMG01000004; CRI32161.1; -; Genomic_DNA.
DR RefSeq; WP_053941482.1; NZ_FZMH01000011.1.
DR AlphaFoldDB; A0A0K2X9Y2; -.
DR STRING; 1578720.HAL011_06060; -.
DR GeneID; 82131623; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000038622; Unassembled WGS sequence.
DR Proteomes; UP000041394; Unassembled WGS sequence.
DR Proteomes; UP000043437; Unassembled WGS sequence.
DR Proteomes; UP000045175; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
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; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 15..312
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 108..288
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 314 AA; 34968 MW; 6B5CBC0856454D76 CRC64;
MKPLAVFLEA HSLGRKNKLD ALGEFVELVS YPGTPQDLVL ERCKDAEIVI LNKVQMSGDT
LRKLPKLKCI CITATGMNMI DLEVAKELGI AIKNVVGYST HSVTMHTFAL AFTLLSNMPY
YDRYCKSGEY CKSEIFTHFN KDLMSLENKE WGIIGLGNIG KNVARIAVSF GAHVSYTSTS
GRNNDSTYPQ KPLEALLKES DVISIHAPLN AQTHNLIDSQ ELKLLKEKAI LINVGRGGIV
NEEAVAKELE VQDFYYATDV LEQEPMRANH PFLNPAIQNK LLITPHIAWG YGDTIKKLII
ATIDNVKDYL KTRG
//
