ID D2QLU0_SPILD Unreviewed; 272 AA.
AC D2QLU0;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 81.
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 OrderedLocusNames=Slin_4399 {ECO:0000313|EMBL:ADB40380.1};
OS Spirosoma linguale (strain ATCC 33905 / DSM 74 / LMG 10896 / Claus 1).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=504472 {ECO:0000313|EMBL:ADB40380.1, ECO:0000313|Proteomes:UP000002028};
RN [1] {ECO:0000313|Proteomes:UP000002028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33905 / DSM 74 / LMG 10896
RC {ECO:0000313|Proteomes:UP000002028};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA Mikhailova N., Ovchinnikova G., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Tindal B., Schutze A., Schneider S.,
RA Goker M., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Spirosoma linguale DSM 74.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADB40380.1, ECO:0000313|Proteomes:UP000002028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33905 / DSM 74 / LMG 10896
RC {ECO:0000313|Proteomes:UP000002028};
RX PubMed=21304700;
RA Lail K., Sikorski J., Saunders E., Lapidus A., Glavina Del Rio T.,
RA Copeland A., Tice H., Cheng J.-F., Lucas S., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.-J.,
RA Jeffries C.D., Chain P., Brettin T., Detter J.C., Schuetze A., Rohde M.,
RA Tindall B.J., Goeker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.-P., Chen F.;
RT "Complete genome sequence of Spirosoma linguale type strain (1).";
RL Stand. Genomic Sci. 2:176-185(2010).
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; CP001769; ADB40380.1; -; Genomic_DNA.
DR AlphaFoldDB; D2QLU0; -.
DR STRING; 504472.Slin_4399; -.
DR KEGG; sli:Slin_4399; -.
DR eggNOG; COG0413; Bacteria.
DR HOGENOM; CLU_036645_1_0_10; -.
DR UniPathway; UPA00028; UER00003.
DR Proteomes; UP000002028; Chromosome.
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:ADB40380.1};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655,
KW ECO:0000256|HAMAP-Rule:MF_00156};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00156}.
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156,
FT ECO:0000256|PIRSR:PIRSR000388-1"
FT BINDING 52..53
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 52
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 91
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 91
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 121
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 123
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 272 AA; 29529 MW; 47F96B5A74D43316 CRC64;
MSVHNPDIKR VTTHTIQELK NKGEKISALT AYDYSMAKAV DAAGVELILV GDSASNVMAG
HETTLPITLD QMIYHACSVV RGVKRALVVV DLPFGSYQGN STEALRSAIR IMKESGAHAV
KMEGGLEIKE SIVRILSAGV PVMGHLGLTP QSIYKFGTYA VRAKEEAEAQ KLIDDAHMLE
DIGCFGLVLE KIPAALTKTV SESLTIPTIG IGAGPDADGQ ILVVHDLLGI TNEFKPRFLR
RYADLHKIMT EAIAHYVDDV KTNDFPNEKE AY
//
