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Database: UniProt
Entry: N2A050_9FIRM
LinkDB: N2A050_9FIRM
Original site: N2A050_9FIRM 
ID   N2A050_9FIRM            Unreviewed;       275 AA.
AC   N2A050;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 58.
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=C823_01920 {ECO:0000313|EMBL:EMZ28553.1}, C823_04505
GN   {ECO:0000313|EMBL:EMZ21506.1};
OS   Eubacterium plexicaudatum ASF492.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=1235802 {ECO:0000313|EMBL:EMZ21506.1, ECO:0000313|Proteomes:UP000012589};
RN   [1] {ECO:0000313|EMBL:EMZ21506.1, ECO:0000313|Proteomes:UP000012589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ASF492 {ECO:0000313|EMBL:EMZ21506.1,
RC   ECO:0000313|Proteomes:UP000012589};
RX   PubMed=24723722;
RA   Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT   "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT   community from gnotobiotic mice.";
RL   Genome Announc. 2:e00287-e00214(2014).
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:EMZ21506.1}.
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DR   EMBL; AQFT01000132; EMZ21506.1; -; Genomic_DNA.
DR   EMBL; AQFT01000063; EMZ28553.1; -; Genomic_DNA.
DR   RefSeq; WP_004059228.1; NZ_AQFT02000004.1.
DR   AlphaFoldDB; N2A050; -.
DR   STRING; 1235802.C823_01920; -.
DR   GeneID; 78438369; -.
DR   PATRIC; fig|1235802.3.peg.2031; -.
DR   eggNOG; COG0413; Bacteria.
DR   HOGENOM; CLU_036645_1_0_9; -.
DR   OrthoDB; 9781789at2; -.
DR   UniPathway; UPA00028; UER00003.
DR   Proteomes; UP000012589; 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:EMZ21506.1};
KW   Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655,
KW   ECO:0000256|HAMAP-Rule:MF_00156};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012589};
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         44..45
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         44
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         83
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         83
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   275 AA;  29634 MW;  D8218D60AA54DBFF CRC64;
     MKNTSVTFKE AKAKGRKLSM LTAYDYTTAK LVDEAGIDAI LVGDSLGMVM LGYEDTLSVT
     MEDMIHHTAA VARGAKNALL IADMPFMSYQ TSVYDAVVNA GRLMKEGRAQ AVKLEGGMEV
     CEHIRAIVKA SIPVCAHLGL TPQSVNAFGG FKVQGKGEEA AQRILDEARA IEEAGAFAVV
     LECVPRALAE KITKSIGIPT IGIGAGAGCD GQVLVYQDML AMYSDMAPKF AKQYDQIGSR
     MKEAFAAYKQ EVADGVFPAE EHTFKMDETI IEKLY
//
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