ID F2AYX6_RHOBT Unreviewed; 320 AA.
AC F2AYX6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|RuleBase:RU362068};
DE EC=1.1.1.169 {ECO:0000256|RuleBase:RU362068};
DE AltName: Full=Ketopantoate reductase {ECO:0000256|RuleBase:RU362068};
GN ORFNames=RBWH47_04712 {ECO:0000313|EMBL:EGF25161.1};
OS Rhodopirellula baltica WH47.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=991778 {ECO:0000313|EMBL:EGF25161.1, ECO:0000313|Proteomes:UP000006222};
RN [1] {ECO:0000313|EMBL:EGF25161.1, ECO:0000313|Proteomes:UP000006222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH47 {ECO:0000313|EMBL:EGF25161.1,
RC ECO:0000313|Proteomes:UP000006222};
RX PubMed=23273849;
RA Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., Richter M.,
RA Achstetter T., Glockner F.O., Harder J.;
RT "Expression of sulfatases in Rhodopirellula baltica and the diversity of
RT sulfatases in the genus Rhodopirellula.";
RL Mar. Genomics 0:0-0(2012).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000256|RuleBase:RU362068}.
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|RuleBase:RU362068};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC {ECO:0000256|RuleBase:RU362068}.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870, ECO:0000256|RuleBase:RU362068}.
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:EGF25161.1}.
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DR EMBL; AFAR01000246; EGF25161.1; -; Genomic_DNA.
DR RefSeq; WP_007328836.1; NZ_AFAR01000246.1.
DR AlphaFoldDB; F2AYX6; -.
DR PATRIC; fig|991778.3.peg.5222; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000006222; 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; IPR003710; ApbA.
DR InterPro; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR00745; apbA_panE; 1.
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 3: Inferred from homology;
KW NADP {ECO:0000256|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068}.
FT DOMAIN 10..157
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 189..310
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 320 AA; 34906 MW; A13D8B6E7B4562FD CRC64;
MTIPAEPLRY AILGSGAVGG LYGAMLARSG CDVHFLLHSD FEHVRENGLR IDSVLGDFVL
ESPQVYDSVE SMPKCDVVII ALKSTRNALL DEWLPRVVAD DGVVLTLQNG LDVEADVRRT
IPAGRVLGGC CFLCSNKVGP GHIHHLDYGR IAFGAYQEPG VDPLRANQVG RRIEADMQSA
GIDANWSDDL AKTRWRKLMW NIPFNGLSVV LDASTDRIIG SQPGRDLANQ LIAEVHAGAA
ACGVEIDEKA IRATMEHTET MVPYDSSMRL DFLAKRPMEV EAIFGNPLRA IGDRASEIAP
SISMLYQQLA FFNDAICQDA
//
