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PANB1_PSEAE
ID   PANB1_PSEAE             Reviewed;         273 AA.
AC   Q9I3C3;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00156};
DE            EC=2.1.2.11 {ECO:0000255|HAMAP-Rule:MF_00156};
DE   AltName: Full=Ketopantoate hydroxymethyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00156};
DE            Short=KPHMT 1 {ECO:0000255|HAMAP-Rule:MF_00156};
GN   Name=panB1 {ECO:0000255|HAMAP-Rule:MF_00156}; OrderedLocusNames=PA1598;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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:0000255|HAMAP-
CC       Rule:MF_00156}.
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; 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-Rule:MF_00156};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantoate from 3-methyl-2-oxobutanoate: step 1/2. {ECO:0000255|HAMAP-
CC       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}.
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DR   EMBL; AE004091; AAG04987.1; -; Genomic_DNA.
DR   PIR; C83447; C83447.
DR   RefSeq; NP_250289.1; NC_002516.2.
DR   RefSeq; WP_003087450.1; NZ_QZGE01000003.1.
DR   AlphaFoldDB; Q9I3C3; -.
DR   SMR; Q9I3C3; -.
DR   STRING; 287.DR97_291; -.
DR   PaxDb; Q9I3C3; -.
DR   DNASU; 882137; -.
DR   EnsemblBacteria; AAG04987; AAG04987; PA1598.
DR   GeneID; 882137; -.
DR   KEGG; pae:PA1598; -.
DR   PATRIC; fig|208964.12.peg.1658; -.
DR   PseudoCAP; PA1598; -.
DR   HOGENOM; CLU_036645_1_0_6; -.
DR   InParanoid; Q9I3C3; -.
DR   OMA; TEDMIGA; -.
DR   PhylomeDB; Q9I3C3; -.
DR   BioCyc; PAER208964:G1FZ6-1628-MON; -.
DR   UniPathway; UPA00028; UER00003.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003864; F:3-methyl-2-oxobutanoate hydroxymethyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IBA:GO_Central.
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;
KW   Cytoplasm; Magnesium; Metal-binding; Pantothenate biosynthesis;
KW   Reference proteome; Transferase.
FT   CHAIN           1..273
FT                   /note="3-methyl-2-oxobutanoate hydroxymethyltransferase 1"
FT                   /id="PRO_0000184874"
FT   ACT_SITE        187
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT   BINDING         49..50
FT                   /ligand="3-methyl-2-oxobutanoate"
FT                   /ligand_id="ChEBI:CHEBI:11851"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT   BINDING         49
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT   BINDING         88
FT                   /ligand="3-methyl-2-oxobutanoate"
FT                   /ligand_id="ChEBI:CHEBI:11851"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT   BINDING         88
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT   BINDING         118
FT                   /ligand="3-methyl-2-oxobutanoate"
FT                   /ligand_id="ChEBI:CHEBI:11851"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT   BINDING         120
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
SQ   SEQUENCE   273 AA;  29802 MW;  B04678CE4EA5E11C CRC64;
     MSSHRPQHRL SVPDIQRRKG AGSLVALTAY STPMARLLDP HADLLLVGDS LGMVLYGMPS
     TLGVSLEMMV AHTLAVMRGS RRACVVADLP FASYQESPRQ AFRNAARLLA DSGAQAVKLE
     GGEEMEETVD FLVRRGIPVL AHIGLMPQQV NAMGGFKAQG RDPESAERVR RDGLAMQRGG
     AFAVVIEGVG EPLARRLSEE LAIPCIGIGA SPACDGQVLV SEDLLGLSGE QVPRFVERYA
     RLDREIDEAA RRFAEDVRER RFPEARHCFA MRE
 
 
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