ID Q9R692_RHIRD Unreviewed; 360 AA.
AC Q9R692;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465};
GN Name=tiorf189 {ECO:0000313|EMBL:BAA87814.1};
OS Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS radiobacter).
OG Plasmid pTi-SAKURA {ECO:0000313|EMBL:BAA87814.1}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=358 {ECO:0000313|EMBL:BAA87814.1};
RN [1] {ECO:0000313|EMBL:BAA87814.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MAFF 301001 {ECO:0000313|EMBL:BAA87814.1};
RC PLASMID=pTi-SAKURA {ECO:0000313|EMBL:BAA87814.1};
RX PubMed=9524202; DOI=10.1016/S0167-4781(97)00182-6;
RA Suzuki K., Ohta N., Hattori Y., Uraji M., Katoh A., Yoshida K.;
RT "Novel structural difference between nopaline- and octopine-type trbJ
RT genes: construction of genetic and physical map and sequencing of trb/traI
RT and rep gene clusters of a new Ti plasmid pTi-SAKURA.";
RL Biochim. Biophys. Acta 1396:1-7(1998).
RN [2] {ECO:0000313|EMBL:BAA87814.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MAFF 301001 {ECO:0000313|EMBL:BAA87814.1};
RC PLASMID=pTi-SAKURA {ECO:0000313|EMBL:BAA87814.1};
RA Hattori Y., Suzuki K., Ohta N., Uraji M., Katoh A., Yoshida K.;
RT "Genome structure of pTi-SAKURA(I): Strategy for DNA sequencing of a
RT Japanese cherry-Ti plasmid.";
RL Nucleic Acids Symp. Ser. 37:159-160(1998).
RN [3] {ECO:0000313|EMBL:BAA87814.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MAFF 301001 {ECO:0000313|EMBL:BAA87814.1};
RC PLASMID=pTi-SAKURA {ECO:0000313|EMBL:BAA87814.1};
RA Ohta N., Suzuki K., Hattori Y., Uraji M., Katoh A., Yoshida K.;
RT "Genome structure of pTi-SAKURA (III): Characteristics of T-DNA.";
RL Nucleic Acids Symp. Ser. 39:185-186(1998).
RN [4] {ECO:0000313|EMBL:BAA87814.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MAFF 301001 {ECO:0000313|EMBL:BAA87814.1};
RC PLASMID=pTi-SAKURA {ECO:0000313|EMBL:BAA87814.1};
RA Uraji M., Suzuki K., Ohta N., Hattori Y., Katoh A., Yoshida K.;
RT "Genome structure of pTi-SAKURA (IV): Characteristics of tra region.";
RL Nucleic Acids Symp. Ser. 39:187-188(1998).
RN [5] {ECO:0000313|EMBL:BAA87814.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MAFF 301001 {ECO:0000313|EMBL:BAA87814.1};
RC PLASMID=pTi-SAKURA {ECO:0000313|EMBL:BAA87814.1};
RA Hattori Y., Suzuki K., Ohta N., Uraji M., Katoh A., Yoshida K.;
RT "Genome structure of pTi-SAKURA (V): Complete nucleotide sequence of
RT plasmid pTi-SAKURA's vir region in Agrobacterium tumefaciens.";
RL Nucleic Acids Symp. Ser. 39:265-266(1998).
RN [6] {ECO:0000313|EMBL:BAA87814.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MAFF 301001 {ECO:0000313|EMBL:BAA87814.1};
RC PLASMID=pTi-SAKURA {ECO:0000313|EMBL:BAA87814.1};
RX PubMed=10721727; DOI=10.1016/S0378-1119(99)00502-8;
RA Suzuki K., Hattori Y., Uraji M., Ohta N., Iwata K., Murata K., Katoh A.,
RA Yoshida K.;
RT "Complete nucleotide sequence of a plant tumor-inducing Ti plasmid.";
RL Gene 242:331-336(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH;
CC Xref=Rhea:RHEA:16233, ChEBI:CHEBI:11561, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15980, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.169; Evidence={ECO:0000256|ARBA:ARBA00000784};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004994}.
CC -!- SIMILARITY: Belongs to the lysopine/nopaline/octopine/opine/vitopine
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00008730}.
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DR EMBL; AB016260; BAA87814.1; -; Genomic_DNA.
DR RefSeq; NP_053429.1; NC_002147.1.
DR RefSeq; WP_010891455.1; NZ_MK439386.1.
DR AlphaFoldDB; Q9R692; -.
DR UniPathway; UPA00028; UER00004.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003421; Opine_DH.
DR PANTHER; PTHR38015; BLR6086 PROTEIN; 1.
DR PANTHER; PTHR38015:SF1; OCTOPINE_DH DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02558; ApbA; 1.
DR Pfam; PF02317; Octopine_DH; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW Plasmid {ECO:0000313|EMBL:BAA87814.1}.
FT DOMAIN 3..100
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 180..322
FT /note="Opine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF02317"
SQ SEQUENCE 360 AA; 38713 MW; 5E26FBC170D01627 CRC64;
MKVGIAGAGS IAIGYAAFLL QNGHEPLIWS RSRERTAAFS AGAPVKITGA ISTEFHPHIC
TNAEELTEAD VIVLALPAYG HRFVLDALLP HLSARHSVII SAHLSFAALY LAKGLAERGI
EIPITAWSTT VLTCKPRAAD TFNIGAIRAK VDMATVPARF AERAHETCVA LFGDRFDVKD
DVLTIALSNL NPQDHMGIAL CNLSRIERAE EWGQNTNVTP AVGRFLEALD LERLAIASAF
GKTVRSTFDH FRLSFDISGQ SVSEISSILV DRGSDPAGPK SLDTRYVLED VPFGLIPTLH
LAKAAGLSAP LHESGVRILS ACYGRDFSEE NDLLPDLGPL DLPTLKKRVV TGYAITAEPV
//
