ID A0A6P0CIG8_9RHOB Unreviewed; 339 AA.
AC A0A6P0CIG8;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 18-JUN-2025, entry version 17.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465};
DE EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014};
DE AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024};
GN ORFNames=GV827_17810 {ECO:0000313|EMBL:NEK24244.1};
OS Sulfitobacter sediminilitoris.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=2698830 {ECO:0000313|EMBL:NEK24244.1, ECO:0000313|Proteomes:UP000468591};
RN [1] {ECO:0000313|EMBL:NEK24244.1, ECO:0000313|Proteomes:UP000468591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBTF-M27 {ECO:0000313|EMBL:NEK24244.1,
RC ECO:0000313|Proteomes:UP000468591};
RA Park S., Yoon J.-H.;
RT "Sulfitobacter sediminilitoris sp. nov., isolated from a tidal flat.";
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantoate + NADP(+) = 2-dehydropantoate + NADPH + H(+);
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:ARBA00048793};
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 ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NEK24244.1}.
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DR EMBL; JAABNT010000013; NEK24244.1; -; Genomic_DNA.
DR RefSeq; WP_164355168.1; NZ_JAABNT010000013.1.
DR AlphaFoldDB; A0A6P0CIG8; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000468591; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
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; IPR050838; Ketopantoate_reductase.
DR InterPro; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 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 NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW Reference proteome {ECO:0000313|Proteomes:UP000468591}.
FT DOMAIN 5..152
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 178..320
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 339 AA; 36123 MW; D0AE23C4972A9623 CRC64;
MAEPVLIWGA GAIGGILGAY WARAGVPVQM VDIVPEHAKA CATTGLTIEG PVEQFTQVVP
CVTPDQLTGT YGRVVLAVKA QATEPALAQL KPHLAENGFV LSAQNGLNER TIARHVGAGR
TMGAFVNYGA DWTGPGRILF GNRGAVVVGE IDGTIRPRTE KMHALLQIFE PEAVLTDDIW
AYLWGKLGYG AMLFATALTA DSMTANFADP ARGPALMGLA REVMQTAVAE GVDPKPFNGF
EPSAFMPGAG DAAALQSLAD LADFNSKTAK THTGIYRDLA VRKRKTEVDP QVGTVAEIAA
SHGIDTPLLR RLVELIHDIE EGRRDMSLDT FHELTKVLT
//
