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Database: UniProt
Entry: A0A0S7BMJ4_9CHLR
LinkDB: A0A0S7BMJ4_9CHLR
Original site: A0A0S7BMJ4_9CHLR 
ID   A0A0S7BMJ4_9CHLR        Unreviewed;       305 AA.
AC   A0A0S7BMJ4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-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=ATC1_131442 {ECO:0000313|EMBL:GAP41453.1};
OS   Flexilinea flocculi.
OC   Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC   Flexilinea.
OX   NCBI_TaxID=1678840 {ECO:0000313|EMBL:GAP41453.1};
RN   [1] {ECO:0000313|EMBL:GAP41453.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC1 {ECO:0000313|EMBL:GAP41453.1};
RA   Matsuura N., Tourlousse D.M., Sun L., Toyonaga M., Kuroda K., Ohashi A.,
RA   Cruz R., Yamaguchi T., Sekiguchi Y.;
RT   "Draft Genome Sequence of Anaerolineae Strain TC1, a Novel Isolate from a
RT   Methanogenic Wastewater Treatment System.";
RL   Genome Announc. 3:e01104-15(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}.
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DR   EMBL; DF968181; GAP41453.1; -; Genomic_DNA.
DR   RefSeq; WP_062282698.1; NZ_DF968181.1.
DR   AlphaFoldDB; A0A0S7BMJ4; -.
DR   STRING; 1678840.ATC1_131442; -.
DR   PATRIC; fig|1678840.3.peg.2906; -.
DR   OrthoDB; 9793586at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000053370; 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:UP000053370}.
FT   DOMAIN          7..151
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          177..302
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   305 AA;  34215 MW;  B4B42709BB3C8DCA CRC64;
     MEIKTVSIIG HGVLGNLFGK IITDHLGKEA VRFVADKDRI ERYQREGVFS NGEKCDFLYM
     DSDAPCEPAD LVIFTVKYLQ LNSAIKTARN QIGDNTIILS LLNGIVSEEI IGKTYGMDKI
     LYSVAQGMDA VKTGNQLTYH LPGRIEFGEA DGSYSDKVKA VDEFFTKAGI AHGMPKDMIK
     KMWSKWMLNV GVNQVVTAYE TTYRETQKEG EARDKFLAAM REVKAIANYK GIDLTEADIQ
     YWVNDVLAPM SPDAMPSMRQ DTLAHRKTEV DLFAGTVIRL GKECGIPTPV NQFLYDRIKE
     IESKF
//
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