ID D0U583_9PSED Unreviewed; 315 AA.
AC D0U583;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 13-SEP-2023, entry version 52.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465, ECO:0000256|RuleBase:RU362068};
DE EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014, ECO:0000256|RuleBase:RU362068};
DE AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024, ECO:0000256|RuleBase:RU362068};
OS Pseudomonas sp. J465.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=674034 {ECO:0000313|EMBL:ACY02001.1};
RN [1] {ECO:0000313|EMBL:ACY02001.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=J465 {ECO:0000313|EMBL:ACY02001.1};
RA Curson A.R.J., Sullivan M.J., Todd J.D., Johnston A.W.B.;
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACY02001.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=J465 {ECO:0000313|EMBL:ACY02001.1};
RX PubMed=19710707; DOI=10.1038/ismej.2009.93;
RA Curson A.R., Sullivan M.J., Todd J.D., Johnston A.W.;
RT "Identification of genes for dimethyl sulfide production in bacteria in the
RT gut of Atlantic Herring (Clupea harengus).";
RL ISME J. 4:144-146(2010).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000256|RuleBase:RU362068}.
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 ECO:0000256|RuleBase:RU362068};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004994, ECO:0000256|RuleBase:RU362068}.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870, ECO:0000256|RuleBase:RU362068}.
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DR EMBL; GQ370384; ACY02001.1; -; Genomic_DNA.
DR AlphaFoldDB; D0U583; -.
DR UniPathway; UPA00028; UER00004.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR003710; ApbA.
DR InterPro; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR00745; apbA_panE; 1.
DR PANTHER; PTHR21708:SF26; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR Pfam; PF02558; ApbA; 1.
DR Pfam; PF08546; ApbA_C; 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 Membrane {ECO:0000256|SAM:Phobius}; NADP {ECO:0000256|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362068};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655,
KW ECO:0000256|RuleBase:RU362068}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 7..156
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 189..310
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 315 AA; 33588 MW; F37B06500DA2BE71 CRC64;
MNAKPRIGII GSGAIGGFYG LMLARAGFDV HFLLRSEFAD VAAHGLQVNS AQHGNLHLKP
VQAYQSVADM PPCDWLLVGA KTTSNAEMAP LIIQAAAPGA KVVLMQNGLA VEEELRPLLP
DSLHLLGGLC YICAHRSAPG VVEHQALGNI NLGYHSGPAN DAESRQLILE QGSALFQAAG
LDSTAMAELD QARWQKLVWN VPYNGLAVLL NSHTTALMSN AESRALVAAI MQEVVDAAAA
CGHQLPAGFA GKLLAATDRM PDYLPSMYHD FILQRPLELH AIYAAPLAAA AAAGCAMPRT
EMLYQALRFL QQRQQ
//
