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Database: UniProt
Entry: A0A2A2GWN2_9GAMM
LinkDB: A0A2A2GWN2_9GAMM
Original site: A0A2A2GWN2_9GAMM 
ID   A0A2A2GWN2_9GAMM        Unreviewed;       389 AA.
AC   A0A2A2GWN2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465};
GN   ORFNames=CBG25_16455 {ECO:0000313|EMBL:PAV01474.1};
OS   Arsenophonus sp. ENCA.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Arsenophonus.
OX   NCBI_TaxID=1987579 {ECO:0000313|EMBL:PAV01474.1, ECO:0000313|Proteomes:UP000217542};
RN   [1] {ECO:0000313|EMBL:PAV01474.1, ECO:0000313|Proteomes:UP000217542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ENCA {ECO:0000313|EMBL:PAV01474.1};
RX   PubMed=28854637; DOI=10.1093/gbe/evx134;
RA   Mao M., Yang X., Poff K., Bennett G.;
RT   "Comparative Genomics of the Dual-Obligate Symbionts from the Treehopper,
RT   Entylia carinata (Hemiptera: Membracidae), Provide Insight into the Origins
RT   and Evolution of an Ancient Symbiosis.";
RL   Genome Biol. Evol. 9:1803-1815(2017).
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:PAV01474.1}.
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DR   EMBL; NHNG01000651; PAV01474.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2GWN2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000217542; 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; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003421; Opine_DH.
DR   PANTHER; PTHR38015; BLR6086 PROTEIN; 1.
DR   PANTHER; PTHR38015:SF1; OCTOPINE_DH DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF02317; Octopine_DH; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217542}.
FT   DOMAIN          9..110
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          197..365
FT                   /note="Opine dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF02317"
SQ   SEQUENCE   389 AA;  43198 MW;  594A5802867140FD CRC64;
     MIAEYKLKVT ICGAGNTGHL AAVLFSQNPK VDVTLFSSQP EFPATYRKNG GQIHALLNDG
     TLLKASPSCV TACPYEACRE ADVIIITTPI HVRDSVLKLI QPALPRNKPV FVGAIPGFGG
     FDWLAEYRLG TLPNIVLWGM KDVSHIAFEL IRGKSVKLGG AKSHLYVALH RREKPEMAEI
     LIGYLNQLYE SPVMLLADYL EITLTPGNPI MHGSVIYGLI GPWGQWHKHS FSHIPCWWND
     CPELGAYFLA RCDEENQLLR KAAEAALHID LSSVQPLQQE IVEAYGDLIA DSRTLLNVLR
     TNQAYEGIPL PLIKAKNEEG YVFDQHHRVF QEDIACGLSL LVAIGKRLNV SVPYINEIYL
     WCCEYIGENS ATVPIPASWP EIRVVTECA
//
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