ID A0A241W5W5_9GAMM Unreviewed; 330 AA.
AC A0A241W5W5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, 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=B9T35_16765 {ECO:0000313|EMBL:OTG88979.1};
OS Acinetobacter sp. ANC 3832.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1977874 {ECO:0000313|EMBL:OTG88979.1, ECO:0000313|Proteomes:UP000194704};
RN [1] {ECO:0000313|EMBL:OTG88979.1, ECO:0000313|Proteomes:UP000194704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 3832 {ECO:0000313|EMBL:OTG88979.1,
RC ECO:0000313|Proteomes:UP000194704};
RA Nemec A., Radolfova-Krizova L.;
RT "High diversity of culturable Acinetobacter species in natural soil and
RT water ecosystems.";
RL Submitted (APR-2017) 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:OTG88979.1}.
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DR EMBL; NEGJ01000019; OTG88979.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A241W5W5; -.
DR STRING; 1977874.B9T35_16765; -.
DR OrthoDB; 6530772at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000194704; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655}.
FT DOMAIN 7..174
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 203..320
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 330 AA; 36601 MW; 5EDA3CBD5DA6A8C6 CRC64;
MGKNAKIAIL GAGAIGCTLA ARLILSGCEC VSLIARGENY QALSSKGIQL KDLTGEYQLI
PYQVVQDIAE LEPQDIIFIA TKSNALHQVA AFIRPVLHAE TVVIPLMNGI PFWYFYQGQS
TDDIQAIQCL DENRQLIKHF PLAHLIGAVV FITARLKGYG KVESDNPYLL ILGEPNNQVT
KRLETIQSLF VDTGIELRVT DQIRDQIWTK VIANLSSNPL SVVTGATLKD VYAHPRLHEM
ALQITQEVRQ VAASYGARIT IDPVTFLQLG TNMGNVHTSM WHDYQKKQPL EMTGIAEAVF
ELAEQFNCPM PVTKHICNLT AYLSEQSLKI
//
