ID I3CG46_9GAMM Unreviewed; 264 AA.
AC I3CG46;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase {ECO:0000256|HAMAP-Rule:MF_00156};
DE EC=2.1.2.11 {ECO:0000256|HAMAP-Rule:MF_00156};
DE AltName: Full=Ketopantoate hydroxymethyltransferase {ECO:0000256|HAMAP-Rule:MF_00156};
DE Short=KPHMT {ECO:0000256|HAMAP-Rule:MF_00156};
GN Name=panB {ECO:0000256|HAMAP-Rule:MF_00156};
GN ORFNames=BegalDRAFT_1711 {ECO:0000313|EMBL:EIJ42589.1};
OS Beggiatoa alba B18LD.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Beggiatoa.
OX NCBI_TaxID=395493 {ECO:0000313|EMBL:EIJ42589.1, ECO:0000313|Proteomes:UP000005744};
RN [1] {ECO:0000313|EMBL:EIJ42589.1, ECO:0000313|Proteomes:UP000005744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B18LD {ECO:0000313|EMBL:EIJ42589.1,
RC ECO:0000313|Proteomes:UP000005744};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Held B., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Samuel K., Teske A.,
RA Mueller J., Woyke T.;
RT "Improved High-Quality Draft sequence of Beggiatoa alba B18lD.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC Rule:MF_00156};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00156,
CC ECO:0000256|PIRSR:PIRSR000388-3};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00156,
CC ECO:0000256|PIRSR:PIRSR000388-3};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 1/2. {ECO:0000256|HAMAP-
CC Rule:MF_00156}.
CC -!- SUBUNIT: Homodecamer; pentamer of dimers.
CC {ECO:0000256|ARBA:ARBA00011424, ECO:0000256|HAMAP-Rule:MF_00156}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00156}.
CC -!- SIMILARITY: Belongs to the PanB family. {ECO:0000256|ARBA:ARBA00008676,
CC ECO:0000256|HAMAP-Rule:MF_00156}.
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DR EMBL; JH600070; EIJ42589.1; -; Genomic_DNA.
DR RefSeq; WP_002685667.1; NZ_JH600070.1.
DR AlphaFoldDB; I3CG46; -.
DR STRING; 395493.BegalDRAFT_1711; -.
DR eggNOG; COG0413; Bacteria.
DR HOGENOM; CLU_036645_1_0_6; -.
DR OrthoDB; 9781789at2; -.
DR UniPathway; UPA00028; UER00003.
DR Proteomes; UP000005744; Unassembled WGS sequence.
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:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; 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; Phosphoenolpyruvate-binding domains; 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 NCBIfam; TIGR00222; panB; 1.
DR PANTHER; PTHR20881; 3-METHYL-2-OXOBUTANOATE HYDROXYMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR20881:SF0; 3-METHYL-2-OXOBUTANOATE HYDROXYMETHYLTRANSFERASE; 1.
DR Pfam; PF02548; Pantoate_transf; 1.
DR PIRSF; PIRSF000388; Pantoate_hydroxy_MeTrfase; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00156};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00156, ECO:0000256|PIRSR:PIRSR000388-
KW 3};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00156,
KW ECO:0000256|PIRSR:PIRSR000388-3};
KW Methyltransferase {ECO:0000313|EMBL:EIJ42589.1};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655,
KW ECO:0000256|HAMAP-Rule:MF_00156};
KW Reference proteome {ECO:0000313|Proteomes:UP000005744};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00156}.
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156,
FT ECO:0000256|PIRSR:PIRSR000388-1"
FT BINDING 45..46
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156,
FT ECO:0000256|PIRSR:PIRSR000388-2"
FT BINDING 45
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156,
FT ECO:0000256|PIRSR:PIRSR000388-3"
FT BINDING 84
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156,
FT ECO:0000256|PIRSR:PIRSR000388-2"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156,
FT ECO:0000256|PIRSR:PIRSR000388-3"
FT BINDING 113
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156,
FT ECO:0000256|PIRSR:PIRSR000388-2"
FT BINDING 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156,
FT ECO:0000256|PIRSR:PIRSR000388-3"
SQ SEQUENCE 264 AA; 28694 MW; 736EFB240AAD038B CRC64;
MPRLSLNHFR KLKRQGEKFA SLTAYDASFA RVIEEAGIEL VLVGDSLGMV IQGHESTLPV
SIEEMIYHSQ QVHRGSDKML LMVDMPFMSY ATPDTALHNA ARLMREGYAQ IVKLEGGTWL
ADTVKLLTER GIPVCAHLGL MPQSVHQLGG YVVQGRAADD AERLRQDALA LQAAGASMLL
LECIPGKLAA EITQLLTIPV IGIGAGADCD GQILVLYDML GLTAKPPSFS KNFLLEQADI
QAAIISYTQA VKNKTFPTPE QTFS
//
