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Database: UniProt
Entry: A0A176QH31_9MICO
LinkDB: A0A176QH31_9MICO
Original site: A0A176QH31_9MICO 
ID   A0A176QH31_9MICO        Unreviewed;       345 AA.
AC   A0A176QH31;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=AWH69_04455 {ECO:0000313|EMBL:OAB89013.1};
OS   Janibacter melonis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Janibacter.
OX   NCBI_TaxID=262209 {ECO:0000313|EMBL:OAB89013.1, ECO:0000313|Proteomes:UP000076976};
RN   [1] {ECO:0000313|EMBL:OAB89013.1, ECO:0000313|Proteomes:UP000076976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD11-4 {ECO:0000313|EMBL:OAB89013.1,
RC   ECO:0000313|Proteomes:UP000076976};
RA   Nair G.R., Kaur G., Chander A.M., Mayilraj S.;
RT   "Janibacter melonis strain CD11_4 genome sequencing and assembly.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:OAB89013.1}.
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DR   EMBL; LQZG01000001; OAB89013.1; -; Genomic_DNA.
DR   RefSeq; WP_068272021.1; NZ_LQZG01000001.1.
DR   AlphaFoldDB; A0A176QH31; -.
DR   STRING; 262209.AWH69_04455; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000076976; 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:UP000076976}.
FT   DOMAIN          3..160
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          182..320
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   345 AA;  36386 MW;  BA561CCE516E2D0A CRC64;
     MRIAVVGAGS IGCYIGAHLA SVADVTLVGR ARVVDAICEQ GLTATTMRGT AWHVPADRLH
     LDTEVSAVSG AEVVLVTTKT VTNHDIAAQI GPYLTTDTVV ISLQNGVRNA QVLDEGLQRA
     FPSRASRPLV LSAVVHHNVV ATDDAVYLAT TSGGITVKDH PRVDPFVRTA RRGGLSVAVE
     PDMRPVLMNK LLLNLNNAVN ALSGRPLRDE LRDPDYRRVL AACQAEALAV SKAAGVTPSR
     MGPLPAALMP AVLRSPTPVF AGLARTSLAV TPQARSSMAD DLGRHRRTEI DELQGMVVAL
     GERYGIATPV SERLVELVVA AEGQSISDGE HRTYTGGELR AAVGL
//
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