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Database: UniProt
Entry: A0A0S7ZCH3_9BACT
LinkDB: A0A0S7ZCH3_9BACT
Original site: A0A0S7ZCH3_9BACT 
ID   A0A0S7ZCH3_9BACT        Unreviewed;       336 AA.
AC   A0A0S7ZCH3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   13-SEP-2023, entry version 21.
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=AMS19_00265 {ECO:0000313|EMBL:KPJ84527.1};
OS   Gemmatimonas sp. SG8_23.
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatimonas.
OX   NCBI_TaxID=1703356 {ECO:0000313|EMBL:KPJ84527.1, ECO:0000313|Proteomes:UP000051174};
RN   [1] {ECO:0000313|EMBL:KPJ84527.1, ECO:0000313|Proteomes:UP000051174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_23 {ECO:0000313|EMBL:KPJ84527.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPJ84527.1}.
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DR   EMBL; LJNO01000002; KPJ84527.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S7ZCH3; -.
DR   PATRIC; fig|1703356.3.peg.2788; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000051174; 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}.
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   336 AA;  36105 MW;  8EA165084F983AF8 CRC64;
     MNPPIVVWGA GAMGGTLGAR LARAGHEVLF VDSDPRHVRA IQDRGLRIVG PIDDFTQPVR
     IVQPDRVEPG LGAVLLAVKA HHTEPAIRSI APLLDPAGFV VSVQNGLNES TIADVVGAER
     TVGCFVNYGA DVVEPGVIMR GNRGAVVVGE IDGARSDRIR WLHELFRDFE PAAVLTDNIW
     GYLWGKLAYG SMLFATALAE ASIAEVLAAA EHRAAIIGLA REAMAVAGAL GIRPEAFDGF
     DPGAFAPGAP DTEAHLSLDR LVAFNRESAK SHSGVWRDLA VRKRRTEVDA QIAPIDRLGR
     EVGVDTPLTR VLVDLIHDVE EGRREQSWET LGLLSR
//
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