ID A0A150L7Y1_9BACI Unreviewed; 297 AA.
AC A0A150L7Y1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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 ORFNames=B4102_1221 {ECO:0000313|EMBL:KYD08139.1}, HV406_09700
GN {ECO:0000313|EMBL:MBL5880575.1};
OS Heyndrickxia sporothermodurans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX NCBI_TaxID=46224 {ECO:0000313|EMBL:KYD08139.1, ECO:0000313|Proteomes:UP000075666};
RN [1] {ECO:0000313|EMBL:KYD08139.1, ECO:0000313|Proteomes:UP000075666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4102 {ECO:0000313|EMBL:KYD08139.1,
RC ECO:0000313|Proteomes:UP000075666};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Genome Sequences of Twelve Sporeforming Bacillus Species Isolated from
RT Foods.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBL5880575.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=L1_158 {ECO:0000313|EMBL:MBL5880575.1};
RA Fiedler G., Herbstmann A.-D., Erik B., Franz C.M.A.P., Boehnlein C.;
RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:MBL5880575.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=L1_158 {ECO:0000313|EMBL:MBL5880575.1};
RA Fiedler G., Herbstmann A.-D., Doll E., Wenning M., Brinks E., Kabisch J.,
RA Breitenwieser F., Lappann M., Boehnlein C., Franz C.M.A.P.;
RT "Taxonomic Evaluation of the Heyndrickxia (Basonym Bacillus)
RT sporothermodurans Group (H. sporothermodurans, H. vini, H. oleronia) Based
RT on Whole Genome Sequences.";
RL Microorganisms 9:0-0(2021).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000256|ARBA:ARBA00002919,
CC 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:KYD08139.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LQYN01000034; KYD08139.1; -; Genomic_DNA.
DR EMBL; JABWTV010000052; MBL5880575.1; -; Genomic_DNA.
DR RefSeq; WP_066230034.1; NZ_NAZD01000060.1.
DR AlphaFoldDB; A0A150L7Y1; -.
DR STRING; 46224.B4102_1221; -.
DR PATRIC; fig|46224.3.peg.2456; -.
DR OrthoDB; 9800163at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000075666; Unassembled WGS sequence.
DR Proteomes; UP000714803; 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; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR PANTHER; PTHR43765:SF2; 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, ECO:0000256|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362068};
KW Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000075666}.
FT DOMAIN 3..148
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 174..292
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 297 AA; 34138 MW; AD6D8CC883557067 CRC64;
MRIGILGAGS IGLLFASYLG KQFDVTLFPR RHEQMDLINE KGVTIETLDS TFTTRVRATL
DKNEFNKQEL IIIAVKQYHL ENIQADITNI HNEIPLLFLQ NGKSHLKLIN HLEHESIIVG
SIEHGALKIN ETTVVHNGIG LTKLAPYRGE INRISPLLNW HCEYFQFKTY LDYKEILLKK
LLVNAIINPL TAILKVKNGE LIKNTFFMQI FHDLYNEIIQ LFPELDSKIV LNEIIRICRN
TENNESSMLK DITLQRKTEI DAIVGYILEL AKEKNVQLPL TNMVYGMIKG MEKRGIE
//