(data stored in ACNUC7421 zone)

SWISSPROT: D6ZCH0_SEGRD

ID   D6ZCH0_SEGRD            Unreviewed;       275 AA.
AC   D6ZCH0;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   16-JAN-2019, 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   OrderedLocusNames=Srot_0528 {ECO:0000313|EMBL:ADG97012.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG97012.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG97012.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
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; CP001958; ADG97012.1; -; Genomic_DNA.
DR   RefSeq; WP_013137468.1; NC_014168.1.
DR   STRING; 640132.Srot_0528; -.
DR   EnsemblBacteria; ADG97012; ADG97012; Srot_0528.
DR   KEGG; srt:Srot_0528; -.
DR   eggNOG; ENOG4105CCG; Bacteria.
DR   eggNOG; COG0413; LUCA.
DR   HOGENOM; HOG000078427; -.
DR   KO; K00606; -.
DR   OMA; GHIGLMP; -.
DR   OrthoDB; 916845at2; -.
DR   BioCyc; SROT640132:G1GLH-531-MONOMER; -.
DR   UniPathway; UPA00028; UER00003.
DR   Proteomes; UP000002247; 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; D6ZCH0.
DR   SWISS-2DPAGE; D6ZCH0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
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:ADG97012.1};
KW   Pantothenate biosynthesis {ECO:0000256|HAMAP-Rule:MF_00156,
KW   ECO:0000256|SAAS:SAAS00771245};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00156,
KW   ECO:0000256|SAAS:SAAS00771224, ECO:0000313|EMBL:ADG97012.1}.
FT   REGION       57     58       Alpha-ketoisovalerate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00156,
FT                                ECO:0000256|PIRSR:PIRSR000388-2}.
FT   ACT_SITE    193    193       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00156, ECO:0000256|PIRSR:PIRSR000388-
FT                                1}.
FT   METAL        57     57       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00156, ECO:0000256|PIRSR:PIRSR000388-
FT                                3}.
FT   METAL        96     96       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00156, ECO:0000256|PIRSR:PIRSR000388-
FT                                3}.
FT   METAL       127    127       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00156, ECO:0000256|PIRSR:PIRSR000388-
FT                                3}.
FT   BINDING      96     96       Alpha-ketoisovalerate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00156,
FT                                ECO:0000256|PIRSR:PIRSR000388-2}.
FT   BINDING     125    125       Alpha-ketoisovalerate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00156,
FT                                ECO:0000256|PIRSR:PIRSR000388-2}.
SQ   SEQUENCE   275 AA;  29044 MW;  A7E1E783717933CD CRC64;
     MSVSAAPYAT QTRPRVRISH LHEMKREGRK WAMLTAYDYT TAALLDAADI PVLLVGDSAA
     NVVYGHDTTV SVEADELLPL VRGVARGAQR ALVVADLPFG SYEASPAQAF ETAARFARAG
     AHAVKLEGGE DYAEHISSLS RAGIPVMAHI GFTPQRVNSL SGFRVQGRGD EAETLVHDAI
     AVAEAGAFAV VMEMVPAELA AQITAKLTIP TVGIGAGPDC DAQVLVWQDM AGLTAGRTAK
     FVRRFAELGA ALGEAAREYA RDVESGAFPA PEHSY
//

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