ID A0A7H8PPN4_9FLAO Unreviewed; 297 AA.
AC A0A7H8PPN4;
DT 10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 1.
DT 18-JUN-2025, entry version 15.
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=HN014_17435 {ECO:0000313|EMBL:QKX06621.1};
OS Aquimarina sp. TRL1.
OC Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aquimarina.
OX NCBI_TaxID=2736252 {ECO:0000313|EMBL:QKX06621.1, ECO:0000313|Proteomes:UP000509763};
RN [1] {ECO:0000313|EMBL:QKX06621.1, ECO:0000313|Proteomes:UP000509763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRL1 {ECO:0000313|EMBL:QKX06621.1,
RC ECO:0000313|Proteomes:UP000509763};
RA Ooi M.C., Bridle A.R.;
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QKX06621.1, ECO:0000313|Proteomes:UP000509763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRL1 {ECO:0000313|EMBL:QKX06621.1,
RC ECO:0000313|Proteomes:UP000509763};
RA Goulden E.F., Trotter A., Smith G.;
RT "Aquimarina sp. associated with a cuticular disease of cultured larval
RT spiny lobster.";
RL Submitted (JUN-2020) 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; CP053590; QKX06621.1; -; Genomic_DNA.
DR RefSeq; WP_176030126.1; NZ_CP053590.1.
DR AlphaFoldDB; A0A7H8PPN4; -.
DR KEGG; aqr:HN014_17435; -.
DR Proteomes; UP000509763; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000509763};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..137
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 168..289
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 297 AA; 33110 MW; E6930610C40ABAE9 CRC64;
MSYKVGILGV GAIGTLMASL LYPNKKLSLF LYNRSPKQQL SIFNDKKEKK IPIHVETSLP
EKRKLDFLCI CLKEHQVKNA HTFLTGLIGV ETKVIVIRNG IHHKEALLPY TSERNIIEAV
IDCPVQPIAD GRYEQLNKPV LIINRTAFSE LFISLFSPAD IKINCILDIK TIAWKKLCES
AALGAILCLA GESCWIFKDQ RLVNLHKKLL QEGVQVAIAD GAEIKEPIFI EAIQTKLVNY
PPEKGSSMLS DRKRGAPIEL GAKNQVISSL GKQYAIETPI HDLVCMLLEK TNNNPTS
//
