ID A0A0B3RHF6_9RHOB Unreviewed; 315 AA.
AC A0A0B3RHF6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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};
GN Name=panE {ECO:0000313|EMBL:KHQ50730.1};
GN ORFNames=OA50_04654 {ECO:0000313|EMBL:KHQ50730.1};
OS Mameliella alba.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Mameliella.
OX NCBI_TaxID=561184 {ECO:0000313|EMBL:KHQ50730.1, ECO:0000313|Proteomes:UP000030960};
RN [1] {ECO:0000313|EMBL:KHQ50730.1, ECO:0000313|Proteomes:UP000030960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMTAT08 {ECO:0000313|EMBL:KHQ50730.1,
RC ECO:0000313|Proteomes:UP000030960};
RA Gan H.Y., Muhd D.-D., Mohd Noor M.E., Yeong Y.S., Usup G.;
RT "Genome sequence of Ponticoccus sp. strain UMTAT08 isolated from clonal
RT culture of toxic dinoflagellate Alexandrium tamiyavanichii.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KHQ50730.1}.
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DR EMBL; JSUQ01000022; KHQ50730.1; -; Genomic_DNA.
DR RefSeq; WP_043145580.1; NZ_JSUQ01000022.1.
DR AlphaFoldDB; A0A0B3RHF6; -.
DR STRING; 561184.SAMN05216376_111103; -.
DR PATRIC; fig|1515334.3.peg.4679; -.
DR OrthoDB; 9793586at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000030960; Unassembled WGS sequence.
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 NADP {ECO:0000256|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362068,
KW ECO:0000313|EMBL:KHQ50730.1};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655,
KW ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000030960}.
FT DOMAIN 3..152
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 178..303
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 315 AA; 32460 MW; BA91DF943B9B5D66 CRC64;
MDIAVLGAGS LGSTIGGRLA QSGHAVTLIN RNAAYVDRVT RAGLILDEGG RRDVIRLEAR
QKPDGGSPVD LLIVLVKSYH TEEAIRAARA LIGPATTVLS LQNGLGQEDI LSAVIGPERV
IAGKTYVGGV MSAPGVIAAG TLGKETIIGE LSGALTPRVQ AIAQAFDAAG LRCIASPNIR
GAMWDKLLVN VATGALAAIT RLNYGNLYDI PEIADTAIAA VAEAMQVAAA LEISLTTTDP
RHAWDKAAKG LGFGFKTSML QSLEKGAPTE IDFVNGAVAR LGRGVAVPTP VNDTLVACIK
GIERALSPKM EGQAA
//
