PANB_NEIMB
ID PANB_NEIMB Reviewed; 263 AA.
AC Q9JZW6;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
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}; OrderedLocusNames=NMB0870;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-263 IN COMPLEX WITH SUBSTRATE
RP AND SODIUM ION, AND SUBUNIT.
RX PubMed=16021622; DOI=10.1002/prot.20541;
RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., Bergseid M.G.,
RA Buchanan S.G., Buchanan M.D., Batiyenko Y., Christopher J.A., Emtage S.,
RA Eroshkina A., Feil I., Furlong E.B., Gajiwala K.S., Gao X., He D.,
RA Hendle J., Huber A., Hoda K., Kearins P., Kissinger C., Laubert B.,
RA Lewis H.A., Lin J., Loomis K., Lorimer D., Louie G., Maletic M.,
RA Marsh C.D., Miller I., Molinari J., Muller-Dieckmann H.J., Newman J.M.,
RA Noland B.W., Pagarigan B., Park F., Peat T.S., Post K.W., Radojicic S.,
RA Ramos A., Romero R., Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J.,
RA Winhoven J., Wright T.A., Wu L., Xu J., Harris T.J.R.;
RT "Structural analysis of a set of proteins resulting from a bacterial
RT genomics project.";
RL Proteins 60:787-796(2005).
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.
CC {ECO:0000305|PubMed:16021622}.
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; AE002098; AAF41281.1; -; Genomic_DNA.
DR PIR; F81148; F81148.
DR RefSeq; NP_273911.1; NC_003112.2.
DR RefSeq; WP_002222670.1; NC_003112.2.
DR PDB; 1O66; X-ray; 1.75 A; A/B/C/D/E=2-263.
DR PDB; 1O68; X-ray; 2.10 A; A/B/C/D/E=2-263.
DR PDBsum; 1O66; -.
DR PDBsum; 1O68; -.
DR AlphaFoldDB; Q9JZW6; -.
DR SMR; Q9JZW6; -.
DR STRING; 122586.NMB0870; -.
DR DrugBank; DB04074; alpha-Ketoisovalerate.
DR PaxDb; Q9JZW6; -.
DR EnsemblBacteria; AAF41281; AAF41281; NMB0870.
DR KEGG; nme:NMB0870; -.
DR PATRIC; fig|122586.8.peg.1083; -.
DR HOGENOM; CLU_036645_1_0_4; -.
DR OMA; VLVWTDM; -.
DR UniPathway; UPA00028; UER00003.
DR EvolutionaryTrace; Q9JZW6; -.
DR Proteomes; UP000000425; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Magnesium; Metal-binding;
KW Pantothenate biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..263
FT /note="3-methyl-2-oxobutanoate hydroxymethyltransferase"
FT /id="PRO_0000184867"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 43..44
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 82
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT BINDING 82
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 111
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT HELIX 4..13
FT /evidence="ECO:0007829|PDB:1O66"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:1O66"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:1O66"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:1O66"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:1O66"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1O66"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:1O66"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:1O66"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1O66"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:1O66"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:1O66"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1O66"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:1O66"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:1O66"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1O66"
FT HELIX 158..170
FT /evidence="ECO:0007829|PDB:1O66"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:1O66"
FT HELIX 183..192
FT /evidence="ECO:0007829|PDB:1O66"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:1O66"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:1O66"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:1O66"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:1O66"
FT HELIX 238..250
FT /evidence="ECO:0007829|PDB:1O66"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:1O66"
SQ SEQUENCE 263 AA; 27739 MW; B863D8238F320317 CRC64;
MITVNTLQKM KAAGEKIAML TAYESSFAAL MDDAGVEMLL VGDSLGMAVQ GRKSTLPVSL
RDMCYHTECV ARGAKNAMIV SDLPFGAYQQ SKEQAFAAAA ELMAAGAHMV KLEGGVWMAE
TTEFLQMRGI PVCAHIGLTP QSVFAFGGYK VQGRGGKAQA LLNDAKAHDD AGAAVVLMEC
VLAELAKKVT ETVSCPTIGI GAGADCDGQV LVMHDMLGIF PGKTAKFVKN FMQGHDSVQA
AVRAYVAEVK AKTFPAAEHI FAD
