(data stored in ACNUC7421 zone)

SWISSPROT: C8W3T9_DESAS

ID   C8W3T9_DESAS            Unreviewed;       280 AA.
AC   C8W3T9;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   16-JAN-2019, entry version 68.
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=Dtox_0240 {ECO:0000313|EMBL:ACV61193.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61193.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61193.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl
CC       group from 5,10-methylenetetrahydrofolate is transferred onto
CC       alpha-ketoisovalerate to form ketopantoate. {ECO:0000256|HAMAP-
CC       Rule:MF_00156, ECO:0000256|SAAS:SAAS00843518}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-
CC         2-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, ECO:0000256|SAAS:SAAS01125081};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00156, ECO:0000256|PIRSR:PIRSR000388-3};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00156, ECO:0000256|PIRSR:PIRSR000388-3};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis;
CC       (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
CC       {ECO:0000256|HAMAP-Rule:MF_00156, ECO:0000256|SAAS:SAAS00771269}.
CC   -!- SUBUNIT: Homodecamer; pentamer of dimers. {ECO:0000256|HAMAP-
CC       Rule:MF_00156, ECO:0000256|SAAS:SAAS00771257}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00156,
CC       ECO:0000256|SAAS:SAAS00771239}.
CC   -!- SIMILARITY: Belongs to the PanB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00156, ECO:0000256|SAAS:SAAS00771235}.
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DR   EMBL; CP001720; ACV61193.1; -; Genomic_DNA.
DR   RefSeq; WP_015755914.1; NC_013216.1.
DR   STRING; 485916.Dtox_0240; -.
DR   EnsemblBacteria; ACV61193; ACV61193; Dtox_0240.
DR   KEGG; dae:Dtox_0240; -.
DR   eggNOG; ENOG4105CCG; Bacteria.
DR   eggNOG; COG0413; LUCA.
DR   HOGENOM; HOG000078427; -.
DR   KO; K00606; -.
DR   OMA; GHIGLMP; -.
DR   OrthoDB; 916845at2; -.
DR   BioCyc; DACE485916:G1GFV-245-MONOMER; -.
DR   UniPathway; UPA00028; UER00003.
DR   Proteomes; UP000002217; 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:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
DR   PRODOM; C8W3T9.
DR   SWISS-2DPAGE; C8W3T9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00156,
KW   ECO:0000256|SAAS:SAAS00771250};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00156,
KW   ECO:0000256|PIRSR:PIRSR000388-3, ECO:0000256|SAAS:SAAS00771249};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00156,
KW   ECO:0000256|PIRSR:PIRSR000388-3, ECO:0000256|SAAS:SAAS00771262};
KW   Methyltransferase {ECO:0000313|EMBL:ACV61193.1};
KW   Pantothenate biosynthesis {ECO:0000256|HAMAP-Rule:MF_00156,
KW   ECO:0000256|SAAS:SAAS00771245};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00156,
KW   ECO:0000256|SAAS:SAAS00771224, ECO:0000313|EMBL:ACV61193.1}.
FT   REGION       47     48       Alpha-ketoisovalerate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00156,
FT                                ECO:0000256|PIRSR:PIRSR000388-2}.
FT   ACT_SITE    185    185       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00156, ECO:0000256|PIRSR:PIRSR000388-
FT                                1}.
FT   METAL        47     47       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00156, ECO:0000256|PIRSR:PIRSR000388-
FT                                3}.
FT   METAL        86     86       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00156, ECO:0000256|PIRSR:PIRSR000388-
FT                                3}.
FT   METAL       118    118       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00156, ECO:0000256|PIRSR:PIRSR000388-
FT                                3}.
FT   BINDING      86     86       Alpha-ketoisovalerate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00156,
FT                                ECO:0000256|PIRSR:PIRSR000388-2}.
FT   BINDING     116    116       Alpha-ketoisovalerate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00156,
FT                                ECO:0000256|PIRSR:PIRSR000388-2}.
SQ   SEQUENCE   280 AA;  30047 MW;  66467025639FEF08 CRC64;
     MTGSKVTTAT FRNMKQEKRP VTMLTVYDYP MAKMLDAAGI DALLVGDSLG NVVLGYDSTI
     PVTMDDMVHH VKAVCRGVQK AMVVADMPFL SYHLSRETAV KNAGRFLQEA GAQAVKLEGG
     IEVCENVRAI VNAGIPVMGH LGLTPQSVHQ MGGYKVQGKD ETAAEKLLSD ANALVQAGVF
     SIVLECVPVP LAKLVTESVP VTTIGIGAGP FCDGQVLVTH DMLDIYGNKA PKFVKRFASL
     YQIIMDALSA YKEEVQNGSF PSAEYGFSMS NDVLEKIKGQ
//

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