HDPA_CORGB
ID HDPA_CORGB Reviewed; 275 AA.
AC A4QFW4;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Dihydroxyacetone phosphatase {ECO:0000303|PubMed:23108048};
DE EC=3.1.3.- {ECO:0000269|PubMed:23108048};
GN Name=hdpA {ECO:0000303|PubMed:23108048};
GN OrderedLocusNames=cgR_2128 {ECO:0000312|EMBL:BAF55130.1};
OS Corynebacterium glutamicum (strain R).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=340322;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R;
RX PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT "Comparative analysis of the Corynebacterium glutamicum group and complete
RT genome sequence of strain R.";
RL Microbiology 153:1042-1058(2007).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=R;
RX PubMed=23108048; DOI=10.1016/j.febslet.2012.10.028;
RA Jojima T., Igari T., Gunji W., Suda M., Inui M., Yukawa H.;
RT "Identification of a HAD superfamily phosphatase, HdpA, involved in 1,3-
RT dihydroxyacetone production during sugar catabolism in Corynebacterium
RT glutamicum.";
RL FEBS Lett. 586:4228-4232(2012).
CC -!- FUNCTION: Catalyzes dephosphorylation of dihydroxyacetone phosphate
CC (DHAP) to produce 1,3-dihydroxyacetone (DHA). Is the main enzyme
CC responsible for DHA production from catabolism of sugars (glucose,
CC fructose, and sucrose) in C.glutamicum. Displays no activity toward
CC nucleoside monophosphates (AMP, CMP, GMP, or UMP).
CC {ECO:0000269|PubMed:23108048}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydroxyacetone phosphate + H2O = dihydroxyacetone +
CC phosphate; Xref=Rhea:RHEA:51728, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16016, ChEBI:CHEBI:43474, ChEBI:CHEBI:57642;
CC Evidence={ECO:0000269|PubMed:23108048};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:23108048};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=Does not show typical Michaelis-Menten type saturation kinetics
CC even when DHAP concentration is increased to 38 mM, suggesting that
CC substrate affinity of HdpA to DHAP is relatively low. This
CC characteristic of HdpA seems to be consistent with the hypothesis of
CC the overflow metabolism, according to which DHA is formed by the
CC action of HdpA only when excess DHAP accumulates in cells.
CC {ECO:0000305|PubMed:23108048};
CC pH dependence:
CC Optimum pH is 5.5-8.0. {ECO:0000269|PubMed:23108048};
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:23108048}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of hdpA leads to a drastic decrease
CC in DHA production from each of glucose, fructose, and sucrose. No
CC dihydroxyacetone phosphatase activity is detected in the deletion
CC mutant strain. {ECO:0000269|PubMed:23108048}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000305}.
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DR EMBL; AP009044; BAF55130.1; -; Genomic_DNA.
DR RefSeq; WP_003857003.1; NC_009342.1.
DR AlphaFoldDB; A4QFW4; -.
DR SMR; A4QFW4; -.
DR EnsemblBacteria; BAF55130; BAF55130; cgR_2128.
DR GeneID; 58311269; -.
DR KEGG; cgt:cgR_2128; -.
DR HOGENOM; CLU_043473_1_1_11; -.
DR OMA; MDGVLIH; -.
DR PhylomeDB; A4QFW4; -.
DR Proteomes; UP000006698; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
DR GO; GO:0016052; P:carbohydrate catabolic process; IMP:UniProtKB.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006357; HAD-SF_hydro_IIA.
DR InterPro; IPR023214; HAD_sf.
DR Pfam; PF13344; Hydrolase_6; 1.
DR PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01460; HAD-SF-IIA; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding.
FT CHAIN 1..275
FT /note="Dihydroxyacetone phosphatase"
FT /id="PRO_0000439281"
FT ACT_SITE 10
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P0AF24"
FT ACT_SITE 12
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AF24"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0AF24"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0AF24"
FT BINDING 206
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0AF24"
FT SITE 56
FT /note="Orients Asp-12 for proton transfer during catalytic
FT turnover"
FT /evidence="ECO:0000250|UniProtKB:P0AF24"
SQ SEQUENCE 275 AA; 29540 MW; AA78244763341FDF CRC64;
MTVNISYLTD MDGVLIKEGE MIPGADRFLQ SLTDNNVEFM VLTNNSIFTP RDLSARLKTS
GLDIPPERIW TSATATAHFL KSQVKEGTAY VVGESGLTTA LHTAGWILTD ANPEFVVLGE
TRTYSFEAIT TAINLILGGA RFICTNPDVT GPSPSGILPA TGSVAALITA ATGAEPYYIG
KPNPVMMRSA LNTIGAHSEH TVMIGDRMDT DVKSGLEAGL STVLVRSGIS DDAEIRRYPF
RPTHVINSIA DLADCWDDPF GDGAFHVPDE QQFTD
