(data stored in ACNUC7421 zone)

SWISSPROT: PANB_RUEPO

ID   PANB_RUEPO              Reviewed;         279 AA.
AC   Q5LWP5;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 85.
DE   RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00156};
DE            EC=2.1.2.11 {ECO:0000255|HAMAP-Rule:MF_00156};
DE   AltName: Full=Ketopantoate hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00156};
DE            Short=KPHMT {ECO:0000255|HAMAP-Rule:MF_00156};
GN   Name=panB {ECO:0000255|HAMAP-Rule:MF_00156};
GN   OrderedLocusNames=SPO0102;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C.,
RA   Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A.,
RA   Rahe E., Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl
CC       group from 5,10-methylenetetrahydrofolate is transferred onto
CC       alpha-ketoisovalerate to form ketopantoate. {ECO:0000255|HAMAP-
CC       Rule:MF_00156}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-
CC         2-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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00156};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00156};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00156};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis;
CC       (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
CC       {ECO:0000255|HAMAP-Rule:MF_00156}.
CC   -!- SUBUNIT: Homodecamer; pentamer of dimers. {ECO:0000255|HAMAP-
CC       Rule:MF_00156}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00156}.
CC   -!- SIMILARITY: Belongs to the PanB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00156}.
DR   EMBL; CP000031; AAV93433.1; -; Genomic_DNA.
DR   RefSeq; WP_011045875.1; NC_003911.12.
DR   SMR; Q5LWP5; -.
DR   STRING; 246200.SPO0102; -.
DR   EnsemblBacteria; AAV93433; AAV93433; SPO0102.
DR   KEGG; sil:SPO0102; -.
DR   eggNOG; ENOG4105CCG; Bacteria.
DR   eggNOG; COG0413; LUCA.
DR   HOGENOM; HOG000078427; -.
DR   KO; K00606; -.
DR   OMA; GHIGLMP; -.
DR   OrthoDB; 916845at2; -.
DR   BioCyc; RPOM246200:G1G48-103-MONOMER; -.
DR   UniPathway; UPA00028; UER00003.
DR   Proteomes; UP000001023; 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   3: Inferred from homology;
DR   PRODOM; Q5LWP5.
DR   SWISS-2DPAGE; Q5LWP5.
KW   Complete proteome; Cytoplasm; Magnesium; Metal-binding;
KW   Pantothenate biosynthesis; Reference proteome; Transferase.
FT   CHAIN         1    279       3-methyl-2-oxobutanoate
FT                                hydroxymethyltransferase.
FT                                /FTId=PRO_0000297379.
FT   REGION       49     50       Alpha-ketoisovalerate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00156}.
FT   ACT_SITE    186    186       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00156}.
FT   METAL        49     49       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00156}.
FT   METAL        88     88       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00156}.
FT   METAL       120    120       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00156}.
FT   BINDING      88     88       Alpha-ketoisovalerate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00156}.
FT   BINDING     118    118       Alpha-ketoisovalerate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00156}.
SQ   SEQUENCE   279 AA;  29171 MW;  CF60DC17256E401D CRC64;
     MSATARKTAP NAQDIRARKG GVPLVSLTAY TTPMARLMDG HCDFVLVGDS VGMVLHGLNS
     TLGVTMEMMI LHGQAVARGL DRAMLVIDMP FASYEEGPAQ AFRNAARLMA ETGAGAVKLE
     GGVEMAETIR FLVKRGIPVM AHIGLTPQSI NTLGGYKVQG RDDQAQAVLA DARAVADAGA
     FSVVLEKVPA TLADRITAEV AIPTIGIGAS AGCDGQILVV DDMLGFFTAF KPKFVKRYAD
     LGPLAEAAIA EYAAEVRARS FPAAEHVFGD QAPAKGAKA
//

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