ID Q7UIB7_RHOBA Unreviewed; 348 AA.
AC Q7UIB7;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Probable 2-dehydropantoate 2-reductase {ECO:0000313|EMBL:CAD77697.1};
DE EC=1.1.1.169 {ECO:0000313|EMBL:CAD77697.1};
GN Name=apbA {ECO:0000313|EMBL:CAD77697.1};
GN OrderedLocusNames=RB12638 {ECO:0000313|EMBL:CAD77697.1};
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD77697.1, ECO:0000313|Proteomes:UP000001025};
RN [1] {ECO:0000313|EMBL:CAD77697.1, ECO:0000313|Proteomes:UP000001025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1
RC {ECO:0000313|Proteomes:UP000001025};
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870}.
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DR EMBL; BX294155; CAD77697.1; -; Genomic_DNA.
DR RefSeq; NP_870620.1; NC_005027.1.
DR RefSeq; WP_007328393.1; NC_005027.1.
DR AlphaFoldDB; Q7UIB7; -.
DR STRING; 243090.RB12638; -.
DR EnsemblBacteria; CAD77697; CAD77697; RB12638.
DR KEGG; rba:RB12638; -.
DR PATRIC; fig|243090.15.peg.6130; -.
DR eggNOG; COG1893; Bacteria.
DR HOGENOM; CLU_796647_0_0_0; -.
DR InParanoid; Q7UIB7; -.
DR OrthoDB; 247668at2; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IBA:GO_Central.
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; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 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 Oxidoreductase {ECO:0000313|EMBL:CAD77697.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001025}.
FT DOMAIN 3..150
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 178..325
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 348 AA; 37350 MW; 25B4DCE6D0BC3F6A CRC64;
MKISVLGAGA IGTMLGGLIR DNDPTCDVVL LGRGGHIQTI RDSGRVRLQG PWPERNVQVI
GTDDPADIAG SDMVLVTVKS QATAEAISAA APYLGAAIVV SVQNGFNDDA LLQHVNEERL
VMGITATNVT VPEPGTASLQ FNGTIVLGPN AQGTNAASAT AATKTLEKTG FRVFEEANVE
GVRYNKLAIN SPGYAASLSQ SNFITEAVCH RGWRSAVGKP LADECLRVFD SAGVKLARIP
KLPDIRKLRG FFGKLDSPLL GPIVGTGAKL IFNRRPIQFS LYQDLLKGKG TEVDHTLGEI
VRLAERNGTT APYNQMVIDL AREIENRGAG KFFTREEVID RFRQIESR
//
