PANB_THEKO
ID PANB_THEKO Reviewed; 284 AA.
AC Q5JCY6;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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, ECO:0000269|PubMed:23941541};
DE AltName: Full=Ketopantoate hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00156, ECO:0000303|PubMed:23941541};
DE Short=KPHMT {ECO:0000255|HAMAP-Rule:MF_00156, ECO:0000303|PubMed:23941541};
GN Name=panB {ECO:0000255|HAMAP-Rule:MF_00156}; OrderedLocusNames=TK0363;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=23941541; DOI=10.1111/mmi.12363;
RA Tomita H., Imanaka T., Atomi H.;
RT "Identification and characterization of an archaeal ketopantoate reductase
RT and its involvement in regulation of coenzyme A biosynthesis.";
RL Mol. Microbiol. 90:307-321(2013).
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-Rule:MF_00156,
CC ECO:0000269|PubMed:23941541}.
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, ECO:0000269|PubMed:23941541};
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 -!- ACTIVITY REGULATION: Neither activated nor inhibited by coenzyme A.
CC {ECO:0000269|PubMed:23941541}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.73 mM for 3-methyl-2-oxobutanoate {ECO:0000269|PubMed:23941541};
CC Note=kcat is 0.76 sec(-1). {ECO:0000269|PubMed:23941541};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00156, ECO:0000305|PubMed:23941541}.
CC -!- SUBUNIT: Homodecamer; pentamer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_00156}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00156,
CC ECO:0000305|PubMed:23941541}.
CC -!- SIMILARITY: Belongs to the PanB family. {ECO:0000255|HAMAP-
CC Rule:MF_00156}.
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DR EMBL; AP006878; BAD84552.1; -; Genomic_DNA.
DR RefSeq; WP_011249318.1; NC_006624.1.
DR AlphaFoldDB; Q5JCY6; -.
DR SMR; Q5JCY6; -.
DR STRING; 69014.TK0363; -.
DR EnsemblBacteria; BAD84552; BAD84552; TK0363.
DR GeneID; 3233895; -.
DR KEGG; tko:TK0363; -.
DR PATRIC; fig|69014.16.peg.360; -.
DR eggNOG; arCOG00584; Archaea.
DR HOGENOM; CLU_036645_1_0_2; -.
DR InParanoid; Q5JCY6; -.
DR OMA; VLVWTDM; -.
DR OrthoDB; 60112at2157; -.
DR PhylomeDB; Q5JCY6; -.
DR BioCyc; MetaCyc:MON-21894; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
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 Coenzyme A biosynthesis; Cytoplasm; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..284
FT /note="3-methyl-2-oxobutanoate hydroxymethyltransferase"
FT /id="PRO_0000184921"
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 44..45
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 44
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 83
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 112
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00156"
SQ SEQUENCE 284 AA; 31743 MW; DDAFD40B3F0ADE20 CRC64;
MREITPRKII EMKGKEKIAM VTAYDYPSAL LADKAGMDIV FVGDSLGMVV YGEPNTLNVS
MEQMVFHTRA VAKAVKRALV LADMPFGSYE VSVEEGVKNA MRLIRAGADA VKIEGGYDHK
KLVKKLVRMG IPVMGHTGLT PQRYLRLGGY RLMGETEEEI EEILRDAKAL EKAGAFAVVL
EFVLADVAKL VTEEVSIPTI GIGAGPHVDG QVLVWHDLLG IYENVPPFVK KYADLASIIQ
LALENYRGEV KEGRFPAKEH YWEFLDKDDF ERKKMKALER LEDE
