PANB_CORGL
ID PANB_CORGL Reviewed; 269 AA.
AC Q9X712;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase;
DE EC=2.1.2.11;
DE AltName: Full=Ketopantoate hydroxymethyltransferase;
DE Short=KPHMT;
GN Name=panB; OrderedLocusNames=Cgl0114, cg0149;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=10223988; DOI=10.1128/aem.65.5.1973-1979.1999;
RA Eggeling L., Sahm H.;
RT "D-pantothenate synthesis in Corynebacterium glutamicum and use of panBC
RT and genes encoding L-valine synthesis for D-pantothenate overproduction.";
RL Appl. Environ. Microbiol. 65:1973-1979(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
CC -!- FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl
CC group from 5,10-methylenetetrahydrofolate is transferred onto alpha-
CC ketoisovalerate to form ketopantoate. {ECO:0000269|PubMed:10223988}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-
CC oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-
CC dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561,
CC ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636,
CC ChEBI:CHEBI:57453; EC=2.1.2.11;
CC Evidence={ECO:0000269|PubMed:10223988};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 1/2.
CC -!- SUBUNIT: Homodecamer; pentamer of dimers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PanB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB97507.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA65397.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAF18682.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X96580; CAA65397.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000036; BAB97507.1; ALT_INIT; Genomic_DNA.
DR EMBL; BX927148; CAF18682.1; ALT_INIT; Genomic_DNA.
DR PIR; T47119; T47119.
DR RefSeq; NP_599367.1; NC_003450.3.
DR RefSeq; WP_011013400.1; NC_006958.1.
DR AlphaFoldDB; Q9X712; -.
DR SMR; Q9X712; -.
DR STRING; 196627.cg0149; -.
DR KEGG; cgb:cg0149; -.
DR KEGG; cgl:Cgl0114; -.
DR PATRIC; fig|196627.13.peg.117; -.
DR eggNOG; COG0413; Bacteria.
DR HOGENOM; CLU_036645_1_0_11; -.
DR OMA; VLVWTDM; -.
DR UniPathway; UPA00028; UER00003.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003864; F:3-methyl-2-oxobutanoate hydroxymethyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06557; KPHMT-like; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR HAMAP; MF_00156; PanB; 1.
DR InterPro; IPR003700; Pantoate_hydroxy_MeTrfase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR20881; PTHR20881; 1.
DR Pfam; PF02548; Pantoate_transf; 1.
DR PIRSF; PIRSF000388; Pantoate_hydroxy_MeTrfase; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR TIGRFAMs; TIGR00222; panB; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Magnesium; Metal-binding; Pantothenate biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..269
FT /note="3-methyl-2-oxobutanoate hydroxymethyltransferase"
FT /id="PRO_0000184838"
FT ACT_SITE 187
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 50..51
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 269 AA; 28324 MW; C494D4FF3D2A0047 CRC64;
MSGIDAKKIR TRHFREAKVN GQKVSVLTSY DALSARIFDE AGVDMLLVGD SAANVVLGRD
TTLSITLDEM IVLAKAVTIA TKRALVVVDL PFGTYEVSPN QAVESAIRVM RETGAAAVKI
EGGVEIAQTI RRIVDAGIPV VGHIGYTPQS EHSLGGHVVQ GRGASSGKLI ADARALEQAG
AFAVVLEMVP AEAAREVTED LSITTIGIGA GNGTDGQVLV WQDAFGLNRG KKPRFVREYA
TLGDSLHDAA QAYIADIHAG TFPGEAESF
