PANE_BACSU
ID PANE_BACSU Reviewed; 298 AA.
AC O34661;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000250|UniProtKB:P0A9J4};
DE EC=1.1.1.169 {ECO:0000250|UniProtKB:P0A9J4};
DE AltName: Full=Ketopantoate reductase {ECO:0000250|UniProtKB:P0A9J4};
DE Short=KPR {ECO:0000250|UniProtKB:P0A9J4};
GN Name=panE; Synonyms=apbA, ylbQ; OrderedLocusNames=BSU15110;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Bertero M., Presecan E., Glaser P., Richou A., Danchin A.;
RT "Bacillus subtilis chromosomal region downstream nprE.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3] {ECO:0007744|PDB:3EGO}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-297.
RA Ramagopal U.A., Toro R., Gilmore M., Hu S., Maletic M., Gheyi T.,
RA Burley S.K., Almo S.C.;
RT "Crystal structure of probable 2-dehydropantoate 2-reductase panE from
RT Bacillus subtilis.";
RL Submitted (SEP-2008) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000250|UniProtKB:P0A9J4}.
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:0000250|UniProtKB:P0A9J4};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC {ECO:0000250|UniProtKB:P0A9J4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A9J4}.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000305}.
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DR EMBL; Z98682; CAB11364.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13384.1; -; Genomic_DNA.
DR PIR; F69875; F69875.
DR RefSeq; NP_389394.1; NC_000964.3.
DR RefSeq; WP_003232206.1; NZ_JNCM01000035.1.
DR PDB; 3EGO; X-ray; 1.90 A; A/B=2-297.
DR PDBsum; 3EGO; -.
DR AlphaFoldDB; O34661; -.
DR SMR; O34661; -.
DR STRING; 224308.BSU15110; -.
DR PaxDb; O34661; -.
DR DNASU; 936782; -.
DR EnsemblBacteria; CAB13384; CAB13384; BSU_15110.
DR GeneID; 936782; -.
DR KEGG; bsu:BSU15110; -.
DR PATRIC; fig|224308.179.peg.1647; -.
DR eggNOG; COG1893; Bacteria.
DR InParanoid; O34661; -.
DR OMA; NYSSMYQ; -.
DR PhylomeDB; O34661; -.
DR BioCyc; BSUB:BSU15110-MON; -.
DR UniPathway; UPA00028; UER00004.
DR EvolutionaryTrace; O34661; -.
DR Proteomes; UP000001570; 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 GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1040.10; -; 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 Pfam; PF02558; ApbA; 1.
DR Pfam; PF08546; ApbA_C; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00745; apbA_panE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; NADP; Oxidoreductase; Pantothenate biosynthesis;
KW Reference proteome.
FT CHAIN 1..298
FT /note="2-dehydropantoate 2-reductase"
FT /id="PRO_0000157311"
FT ACT_SITE 179
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 7..12
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 98
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 124
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 258
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3EGO"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:3EGO"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:3EGO"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:3EGO"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:3EGO"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:3EGO"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:3EGO"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:3EGO"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:3EGO"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:3EGO"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:3EGO"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3EGO"
FT HELIX 101..107
FT /evidence="ECO:0007829|PDB:3EGO"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:3EGO"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:3EGO"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:3EGO"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:3EGO"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:3EGO"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:3EGO"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:3EGO"
FT HELIX 172..193
FT /evidence="ECO:0007829|PDB:3EGO"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:3EGO"
FT HELIX 204..221
FT /evidence="ECO:0007829|PDB:3EGO"
FT HELIX 226..239
FT /evidence="ECO:0007829|PDB:3EGO"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:3EGO"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:3EGO"
FT HELIX 259..272
FT /evidence="ECO:0007829|PDB:3EGO"
FT HELIX 278..289
FT /evidence="ECO:0007829|PDB:3EGO"
SQ SEQUENCE 298 AA; 33287 MW; A0B645A0A415FFD5 CRC64;
MKIGIIGGGS VGLLCAYYLS LYHDVTVVTR RQEQAAAIQS EGIRLYKGGE EFRADCSADT
SINSDFDLLV VTVKQHQLQS VFSSLERIGK TNILFLQNGM GHIHDLKDWH VGHSIYVGIV
EHGAVRKSDT AVDHTGLGAI KWSAFDDAEP DRLNILFQHN HSDFPIYYET DWYRLLTGKL
IVNACINPLT ALLQVKNGEL LTTPAYLAFM KLVFQEACRI LKLENEEKAW ERVQAVCGQT
KENRSSMLVD VIGGRQTEAD AIIGYLLKEA SLQGLDAVHL EFLYGSIKAL ERNTNKVF
