GenomeNet

Database: UniProt
Entry: R5BAJ9_9BACE
LinkDB: R5BAJ9_9BACE
Original site: R5BAJ9_9BACE 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system