ID A0A0P6XIV5_9CHLR Unreviewed; 348 AA.
AC A0A0P6XIV5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|RuleBase:RU362068};
DE EC=1.1.1.169 {ECO:0000256|RuleBase:RU362068};
DE AltName: Full=Ketopantoate reductase {ECO:0000256|RuleBase:RU362068};
GN ORFNames=AC812_10410 {ECO:0000313|EMBL:KPL74926.1};
OS Bellilinea caldifistulae.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Bellilinea.
OX NCBI_TaxID=360411 {ECO:0000313|EMBL:KPL74926.1, ECO:0000313|Proteomes:UP000050514};
RN [1] {ECO:0000313|EMBL:KPL74926.1, ECO:0000313|Proteomes:UP000050514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GOMI-1 {ECO:0000313|EMBL:KPL74926.1,
RC ECO:0000313|Proteomes:UP000050514};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Draft genome of Bellilinea caldifistulae DSM 17877.";
RL Submitted (JUL-2015) 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|RuleBase:RU362068};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC {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:KPL74926.1}.
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DR EMBL; LGHJ01000016; KPL74926.1; -; Genomic_DNA.
DR RefSeq; WP_061915868.1; NZ_LGHJ01000016.1.
DR AlphaFoldDB; A0A0P6XIV5; -.
DR STRING; 360411.AC812_10410; -.
DR PATRIC; fig|360411.5.peg.2698; -.
DR OrthoDB; 9796561at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000050514; 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 Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000050514}.
FT DOMAIN 4..145
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 179..316
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 348 AA; 38430 MW; A10C382AFB4436A2 CRC64;
MNYLIFGMGA IGTYIGGSLK LSGERVFYLE RAEVARRFNQ QPLVVEIDGK EQPFVPDMLS
DSLEAILERY TVDVAVVAVK SFDTPAVASL LKPYCNQVSA VLSLQNGVEN EEILAEFVGN
ERVLAGTLTS AVAKKETGRV VLEKKRGVGI AGDRPLSRKI VESFNRAGLN AKLFPNAGEM
KWSKLITNLL ANASSAILDL TPAEIFSHPK LFKIETEQVR EAVRVMSKLN YRVIDLPGTP
VRLLSLLFHS IPEEIARRVA GKTLAAGRGG KMPSFHVDLY RGHRPLEVDY LNGAVVRFGE
RLGVATPVNL FLNEALLSIA ERPLETNIYR KNPDRLIAVL SERVRLFS
//
