ID G7ZDB1_AZOL4 Unreviewed; 327 AA.
AC G7ZDB1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:CBS89416.1};
DE EC=1.1.1.29 {ECO:0000313|EMBL:CBS89416.1};
GN Name=hprA {ECO:0000313|EMBL:CBS89416.1};
GN OrderedLocusNames=AZOLI_p20254 {ECO:0000313|EMBL:CBS89416.1};
OS Azospirillum lipoferum (strain 4B).
OG Plasmid AZO_p2 {ECO:0000313|EMBL:CBS89416.1,
OG ECO:0000313|Proteomes:UP000005667}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS89416.1, ECO:0000313|Proteomes:UP000005667};
RN [1] {ECO:0000313|Proteomes:UP000005667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RC PLASMID=Plasmid AZO_p2 {ECO:0000313|Proteomes:UP000005667};
RX PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA Zhulin I.B.;
RT "Azospirillum genomes reveal transition of bacteria from aquatic to
RT terrestrial environments.";
RL PLoS Genet. 7:E1002430-E1002430(2011).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; FQ311870; CBS89416.1; -; Genomic_DNA.
DR AlphaFoldDB; G7ZDB1; -.
DR KEGG; ali:AZOLI_p20254; -.
DR HOGENOM; CLU_019796_1_3_5; -.
DR Proteomes; UP000005667; Plasmid AZO_p2.
DR GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd12162; 2-Hacid_dh_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; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW ECO:0000313|EMBL:CBS89416.1}; Plasmid {ECO:0000313|EMBL:CBS89416.1}.
FT DOMAIN 32..322
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 113..293
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 327 AA; 35729 MW; B75D2EFA03A6E03E CRC64;
MTKDIVMRKI VFLDRATLAP QIRLRKPGFP HELVEHAQTT PDQVLDHLAG AEIAIVNKVQ
LTADLLERLP QLKLIAVAAT GTDCVDKEYC RTHGIAVSNI RGYAINTVPE HTFALMLALR
RNIVPFRQDV LDGEWQKSGQ FCFFNHPIHD LQGARLGIIG EGVLGQRVAD IARAFGMVPL
FAAHKGKSGL GPLYTPWDVV LETSDIITLH SPLTPETRGM IAMPEFRQMK RRPLIINTAR
GGLVVEEDLV TALDEGLIGG AGFDVTLPEP PPADSPLMRI AGRPNVIVTP HLGWASDEAQ
QALADQLIDN IENFVAGTPS NLVMGAY
//
