ID A4EHY5_9RHOB Unreviewed; 325 AA.
AC A4EHY5;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 65.
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=RCCS2_12914 {ECO:0000313|EMBL:EBA12198.1};
OS Roseobacter sp. CCS2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=391593 {ECO:0000313|EMBL:EBA12198.1, ECO:0000313|Proteomes:UP000003535};
RN [1] {ECO:0000313|EMBL:EBA12198.1, ECO:0000313|Proteomes:UP000003535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCS2 {ECO:0000313|EMBL:EBA12198.1,
RC ECO:0000313|Proteomes:UP000003535};
RA Mary Ann M.A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004994}.
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:EBA12198.1}.
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DR EMBL; AAYB01000002; EBA12198.1; -; Genomic_DNA.
DR RefSeq; WP_008233050.1; NZ_AAYB01000002.1.
DR AlphaFoldDB; A4EHY5; -.
DR eggNOG; COG1893; Bacteria.
DR OrthoDB; 9796561at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000003535; 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; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR21708:SF42; 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}.
FT DOMAIN 3..169
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 197..316
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 325 AA; 34606 MW; A3E2E4C384DBEB2E CRC64;
MKICIFGAGA IGGYMGAKLA EAGADVSLVA RGPHLAALRE NGLTLIEGGE TRTMPVTVSD
DPADLGPQDY VIVTLKAHSV PPVVDKMKPL IGPDTTIVSG VNGVPWWYFH QIGTDLEGTR
LASVDPGDAQ WNGFGPDSVL GCVVYPAAEV IEPGVIKHIE GNRFSLGEPS GEKSDRAMRL
SKALSAAGLK APVRPKIRDE IWIKLWGNLS FNPISALTHA TLDVLCTDPG TREVARNMML
EAQTIAEKLG VKFPIDVDRR IQGGADVGAH RTSMLQDLDM GRPMEIDALV GSVQELGRVT
DTPTPTIDTV LALVQLRART AGLYS
//
