GRP2_CANAL
ID GRP2_CANAL Reviewed; 341 AA.
AC P83775; A0A1D8PNJ6; Q5AG70;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Putative NADPH-dependent methylglyoxal reductase GRP2;
DE EC=1.1.1.283 {ECO:0000250|UniProtKB:Q12068};
DE AltName: Full=Cytoplasmic antigenic protein 2;
GN Name=GRP2; Synonyms=GRE22; OrderedLocusNames=CAALFM_C502860CA;
GN ORFNames=CaO19.11785, CaO19.4309;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP PROTEIN SEQUENCE OF 128-139 AND 299-305, SUBCELLULAR LOCATION, AND
RP ANTIGENICITY.
RC STRAIN=SC5314 / ATCC MYA-2876; TISSUE=Protoplast;
RX PubMed=15378761; DOI=10.1002/pmic.200400903;
RA Pitarch A., Abian J., Carrascal M., Sanchez M., Nombela C., Gil C.;
RT "Proteomics-based identification of novel Candida albicans antigens for
RT diagnosis of systemic candidiasis in patients with underlying hematological
RT malignancies.";
RL Proteomics 4:3084-3106(2004).
CC -!- FUNCTION: Catalyzes the irreversible reduction of the cytotoxic
CC compound methylglyoxal (MG, 2-oxopropanal) to (S)-lactaldehyde. MG is
CC synthesized via a bypath of glycolysis from dihydroxyacetone phosphate
CC and is believed to play a role in cell cycle regulation and stress
CC adaptation. {ECO:0000250|UniProtKB:Q12068}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactaldehyde + NADP(+) = H(+) + methylglyoxal + NADPH;
CC Xref=Rhea:RHEA:21748, ChEBI:CHEBI:15378, ChEBI:CHEBI:17158,
CC ChEBI:CHEBI:18041, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.283; Evidence={ECO:0000250|UniProtKB:Q12068};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15378761}.
CC -!- MISCELLANEOUS: Has antigenic properties. Elicits a specific immune
CC response in systemic candidiasis human patients undergoing malignant
CC hematological disorders.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
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DR EMBL; CP017627; AOW29710.1; -; Genomic_DNA.
DR RefSeq; XP_720616.1; XM_715523.2.
DR AlphaFoldDB; P83775; -.
DR SMR; P83775; -.
DR STRING; 237561.P83775; -.
DR COMPLUYEAST-2DPAGE; P83775; -.
DR PRIDE; P83775; -.
DR GeneID; 3637744; -.
DR KEGG; cal:CAALFM_C502860CA; -.
DR CGD; CAL0000189861; GRP2.
DR VEuPathDB; FungiDB:C5_02860C_A; -.
DR eggNOG; KOG1502; Eukaryota.
DR HOGENOM; CLU_007383_9_2_1; -.
DR InParanoid; P83775; -.
DR OMA; YAYAKTT; -.
DR OrthoDB; 992332at2759; -.
DR PRO; PR:P83775; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IDA:CGD.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR GO; GO:0043892; F:methylglyoxal reductase (NADPH-dependent) activity; IEA:UniProtKB-EC.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:CGD.
DR GO; GO:0009438; P:methylglyoxal metabolic process; IDA:CGD.
DR GO; GO:0006090; P:pyruvate metabolic process; IDA:CGD.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..341
FT /note="Putative NADPH-dependent methylglyoxal reductase
FT GRP2"
FT /id="PRO_0000089302"
FT BINDING 40
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT BINDING 171
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
SQ SEQUENCE 341 AA; 37634 MW; 0955822432503E47 CRC64;
MSSSTTVFVS GASGFIAQTL VKQLIEKGYK VVGTVRSNEK GDSLKENLKA AKLQSENFTY
EIVKDIAVKG AFDDALKKHP EVTVFLHTAS PFHFNVTDIE KELLTPAVEG TNNALQAIKT
HGPQIKRVVV TSSYAAVGRF ADLADPSIPA TEESWNPITW EQSLSNPLAG YVGSKKFAEK
AAWDFVEKEK PNFTLSVINP VYVFGPQAFE IKNKSQLNTS SEIINGLLNS KPDSKFDNLT
GYFIDVRDVA KAHIVAFEKD SIQGQRLILA ESPFSTQSIL DLIRKDFPQL DSQLPKGDPS
QADAWKKAES KIENEKTREL LGFKFIDFKK SIDDSVAQII G
