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Database: UniProt
Entry: A0A1M4MY34_9RHOB
LinkDB: A0A1M4MY34_9RHOB
Original site: A0A1M4MY34_9RHOB 
ID   A0A1M4MY34_9RHOB        Unreviewed;       320 AA.
AC   A0A1M4MY34;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   18-JUN-2025, entry version 27.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465};
DE            EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014};
DE   AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024};
GN   ORFNames=KARMA_1698 {ECO:0000313|EMBL:SCM67499.1};
OS   Donghicola eburneus.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rhodobacterales; Roseobacteraceae; Donghicola.
OX   NCBI_TaxID=393278 {ECO:0000313|EMBL:SCM67499.1, ECO:0000313|Proteomes:UP000184085};
RN   [1] {ECO:0000313|Proteomes:UP000184085}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wibberg D.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantoate + NADP(+) = 2-dehydropantoate + NADPH + H(+);
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:ARBA00048793};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00004994}.
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DR   EMBL; FMJB01000046; SCM67499.1; -; Genomic_DNA.
DR   RefSeq; WP_072706128.1; NZ_FMJB01000046.1.
DR   AlphaFoldDB; A0A1M4MY34; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000184085; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
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   FunFam; 1.10.1040.10:FF:000017; 2-dehydropantoate 2-reductase; 1.
DR   Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
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; IPR013752; KPA_reductase.
DR   InterPro; IPR051402; KPR-Related.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; NF005089; PRK06522.1-4; 1.
DR   PANTHER; PTHR21708:SF45; 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   4: Predicted;
KW   Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184085}.
FT   DOMAIN          4..104
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          193..310
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   320 AA;  33278 MW;  1C1D76681753067E CRC64;
     MKVSVIGAGA IGGWLTAGFV KGGAEATVLA RGASLAALQN TGLVLEADGT TETIPVTATN
     DPDQLRGADL LLLGVKAHDL PALAPVIEQI MTAETLVMPA VNGLPFWFLS GFGGPAEGKT
     LASVDPGGTL AKLMPVERVV ANVVHAASRV AAPGHIQLVK ANKVILGGQP DGLSDIAACL
     QRGGIPIETT DAIHREVWMK LWGNSNMNPL SALARADAAQ LHDDPGANSV IRTMMQEMAD
     LGVRIGLEGF DDIEGRMATT RKLGPIRTSM LQDVEAGRPF ELGPILGALV ELAELVDQPV
     PMMKGIHGLA GLLDRNLRAV
//
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