ID G7ZA91_AZOL4 Unreviewed; 341 AA.
AC G7ZA91;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
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 Name=panE {ECO:0000313|EMBL:CBS88586.1};
GN OrderedLocusNames=AZOLI_p10301 {ECO:0000313|EMBL:CBS88586.1};
OS Azospirillum lipoferum (strain 4B).
OG Plasmid AZO_p1 {ECO:0000313|EMBL:CBS88586.1,
OG ECO:0000313|Proteomes:UP000005667}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS88586.1, ECO:0000313|Proteomes:UP000005667};
RN [1] {ECO:0000313|Proteomes:UP000005667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RC PLASMID=Plasmid AZO_p1 {ECO:0000313|Proteomes:UP000005667};
RX PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA Zhulin I.B.;
RT "Azospirillum genomes reveal transition of bacteria from aquatic to
RT terrestrial environments.";
RL PLoS Genet. 7:E1002430-E1002430(2011).
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}.
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DR EMBL; FQ311869; CBS88586.1; -; Genomic_DNA.
DR RefSeq; WP_014188043.1; NC_016585.1.
DR AlphaFoldDB; G7ZA91; -.
DR KEGG; ali:AZOLI_p10301; -.
DR HOGENOM; CLU_031468_6_1_5; -.
DR OrthoDB; 247668at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000005667; Plasmid AZO_p1.
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 Oxidoreductase {ECO:0000313|EMBL:CBS88586.1};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW Plasmid {ECO:0000313|EMBL:CBS88586.1}.
FT DOMAIN 3..104
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"
FT REGION 322..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 341 AA; 36180 MW; 057C391665B6A3B3 CRC64;
MKICIYGSGA IGGYLGVRLH QAGAEVSLVA RGAHLAAMRE NGVTLLMGEE KTVVHPRCTD
NPAELGPQDY VIIALKAHSV PGVVPAMQPL LGEDTAVVTA VNGIPYWYFY GTGGAFDGRT
LETVDPGAVQ WKGLGPERAI GCVVYPATEV VEPGVIQHVY GDKFSLGEPD GSTSDRVVAL
SKAMEAGGLR APVLDRIRDE IWLKLWGNLC FNPISALTHG TLEVICGDAE TRAVAKAMML
EAKEIGDRLG VHFRVDVERR INGAAAVGAH KTSMLQDLER GRPMEIDPLL SVVQEMGRMV
GVATPTIDVV LALVKQRGET AGCYSRPQPA AAPAPEVVAA Q
//
