ID R5BAJ9_9BACE Unreviewed; 273 AA.
AC R5BAJ9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=BN813_01609 {ECO:0000313|EMBL:CCX48451.1};
OS Bacteroides sp. CAG:927.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1262753 {ECO:0000313|EMBL:CCX48451.1, ECO:0000313|Proteomes:UP000017907};
RN [1] {ECO:0000313|EMBL:CCX48451.1, ECO:0000313|Proteomes:UP000017907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:927 {ECO:0000313|Proteomes:UP000017907};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCX48451.1}.
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DR EMBL; CAWM010000058; CCX48451.1; -; Genomic_DNA.
DR AlphaFoldDB; R5BAJ9; -.
DR STRING; 1262753.BN813_01609; -.
DR UniPathway; UPA00028; UER00003.
DR Proteomes; UP000017907; 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:CCX48451.1};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655,
KW ECO:0000256|HAMAP-Rule:MF_00156};
KW Reference proteome {ECO:0000313|Proteomes:UP000017907};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00156}.
FT ACT_SITE 191
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156,
FT ECO:0000256|PIRSR:PIRSR000388-1"
FT BINDING 53..54
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 53
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 92
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 92
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 122
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 124
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 273 AA; 29434 MW; BA382B6D50327AE5 CRC64;
MSTYNEQAKP KVTTALLRKM KENGEKIACI TSYDYTMASI VDAAGADFIL VGDSASNVML
GNETTLPITV DEMITYAKGT VRGAKRALVV VDMPFGTYQG DPMGALHNAV RVMRETGAGA
VKMEGGQEIR ESIEKVLCAG IPVCGHLGLT PQSVNKFGGY GVRAKEDAEA ERLLNDAKML
EELGCFAIVL EKIPAQLAAR VTREVNIPII GIGAGSEVDG QIIVVQDMLG MNKGFKPKFL
RVYADMFNAI ENAVGQYVKD VKDVSFPNAN EQY
//