GAR1_HYPJE
ID GAR1_HYPJE Reviewed; 309 AA.
AC Q3ZFI7;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=D-galacturonate reductase;
DE EC=1.1.1.365;
DE AltName: Full=D-galacturonic acid reductase;
GN Name=gar1;
OS Hypocrea jecorina (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=51453;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 232-247 AND 294-309,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=ATCC 56765 / Rut C-30;
RX PubMed=16101307; DOI=10.1021/bi050792f;
RA Kuorelahti S., Kalkkinen N., Penttila M., Londesborough J., Richard P.;
RT "Identification in the mold Hypocrea jecorina of the first fungal D-
RT galacturonic acid reductase.";
RL Biochemistry 44:11234-11240(2005).
CC -!- FUNCTION: Mediates the reduction of D-galacturonate to L-galactonate,
CC the first step in D-galacturonate catabolic process. Also has activity
CC with D-glucuronate and DL-glyceraldehyde. No activity is observed with
CC D-glucose, D-fructose, D-xylose, D-galactose, L-arabinose or D-mannose.
CC Activity is seen only with NADPH and not with NADH.
CC {ECO:0000269|PubMed:16101307}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-galactonate + NADP(+) = aldehydo-D-galacturonate + H(+) +
CC NADPH; Xref=Rhea:RHEA:26345, ChEBI:CHEBI:12952, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:53071, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.365; Evidence={ECO:0000269|PubMed:16101307};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6 mM for D-galacturonate {ECO:0000269|PubMed:16101307};
CC KM=30 uM for NADPH {ECO:0000269|PubMed:16101307};
CC KM=11 mM for D-glucuronate {ECO:0000269|PubMed:16101307};
CC KM=6 mM for DL-glyceraldehyde {ECO:0000269|PubMed:16101307};
CC KM=30 uM for NADP(+) {ECO:0000269|PubMed:16101307};
CC Vmax=40 umol/min/mg enzyme with D-galacturonate acid and NADPH as
CC substrates {ECO:0000269|PubMed:16101307};
CC Vmax=25 umol/min/mg enzyme with D-glucuronate as substrate
CC {ECO:0000269|PubMed:16101307};
CC Vmax=7 umol/min/mg enzyme with DL-glyceraldehyde as substrate
CC {ECO:0000269|PubMed:16101307};
CC -!- PATHWAY: Carbohydrate acid metabolism. {ECO:0000269|PubMed:16101307}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; AY862503; AAX54673.1; -; mRNA.
DR AlphaFoldDB; Q3ZFI7; -.
DR SMR; Q3ZFI7; -.
DR KEGG; ag:AAX54673; -.
DR VEuPathDB; FungiDB:TrQ_005176; -.
DR OMA; WRHPDEP; -.
DR BioCyc; MetaCyc:MON-15601; -.
DR SABIO-RK; Q3ZFI7; -.
DR GO; GO:0102098; F:D-galacturonate reductase 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:UniProtKB.
DR GO; GO:0019698; P:D-galacturonate catabolic process; IDA:UniProtKB.
DR CDD; cd19121; AKR_AKR3D1; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044495; AKR3D.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; NADP; Oxidoreductase.
FT CHAIN 1..309
FT /note="D-galacturonate reductase"
FT /id="PRO_0000425566"
FT ACT_SITE 50
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 210..264
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT CONFLICT 304
FT /note="G -> GFP (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 33997 MW; 113B49F8B24CAA51 CRC64;
MVATSFKLNN GLEIPAVGLG TWQSKAGEVK AAVSYALQIG YKLIDGAYCY GNEDEVGEGL
KEAFAAGVKR EDIFVVTKIW ATYNTRVVLG LDKSLRSLGL DYVDLLLVHW PVLLNPEGNH
DKFPTLPDGK RDVIWDYNHV DGWKQMEAVL ATGKTKSIGV SNYSKKYLEQ LLPHATVIPA
VNQIENHPSL PQQEIVDFCK EKGIHIMAYS PLGSTGSPLM SADPVVKIAE KKGISPTTVL
LSYHVNRGST VLAKSVTPAR IKANLEIVDL DDEDMKLLND YSNDLASKGE LKRYVYPPFG
IDFGFPDKS
