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Database: UniProt
Entry: A0A0I9TDJ9_9MYCO
LinkDB: A0A0I9TDJ9_9MYCO
Original site: A0A0I9TDJ9_9MYCO 
ID   A0A0I9TDJ9_9MYCO        Unreviewed;       267 AA.
AC   A0A0I9TDJ9;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=ABH38_18555 {ECO:0000313|EMBL:KLO34533.1};
OS   Mycobacterium haemophilum.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=29311 {ECO:0000313|EMBL:KLO34533.1, ECO:0000313|Proteomes:UP000036334};
RN   [1] {ECO:0000313|EMBL:KLO34533.1, ECO:0000313|Proteomes:UP000036334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UC1 {ECO:0000313|Proteomes:UP000036334};
RA   Greninger A.L., Cunningham G., Miller S.;
RT   "Genome sequence of Mycobacterium haemophilum.";
RL   Submitted (MAY-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:KLO34533.1}.
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DR   EMBL; LDPR01000025; KLO34533.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0I9TDJ9; -.
DR   STRING; 1202450.B586_13830; -.
DR   PATRIC; fig|29311.18.peg.2929; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000036334; 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   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.
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:UP000036334}.
FT   DOMAIN          17..118
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          141..260
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   267 AA;  28669 MW;  C096403FB53634FA CRC64;
     MVCGHTPRDS IELRPDGNHR IVVPGPVRTD PGEVTGPVDV VVLAVKATQN DDVRGWLTGL
     CDEHTIVTVL QNGVEQVEQV QPLCPSSAVV PGIVWYSAET QPQGWVRLRG EAALVLPTGP
     EAETVAELLR GAGCRVDCDP DFHTAAWRKL LVNALAGFMA LSGRRSGMFR RDDVAALSRR
     YVAECLAVAQ AEGARLADDA VDELVGLFGQ APEDMGTSIL ADRENHRRLE WDIRNGVIIR
     KARVHNLATP ISDVVVPLLG AASDGPG
//
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