ID M5D3B3_STEMA Unreviewed; 276 AA.
AC M5D3B3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 08-NOV-2023, entry version 28.
DE SubName: Full=3-methyl-2-oxobutanoatehydroxymethyltransferase {ECO:0000313|EMBL:CCP18613.1};
DE EC=2.1.2.11 {ECO:0000313|EMBL:CCP18613.1};
GN ORFNames=SMRA8_4157 {ECO:0000313|EMBL:CCP18613.1};
OS Stenotrophomonas maltophilia RA8.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=1118157 {ECO:0000313|EMBL:CCP18613.1, ECO:0000313|Proteomes:UP000012177};
RN [1] {ECO:0000313|EMBL:CCP18613.1, ECO:0000313|Proteomes:UP000012177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA8 {ECO:0000313|EMBL:CCP18613.1,
RC ECO:0000313|Proteomes:UP000012177};
RA Linke B., Adamek M., Schwartz T.;
RT "Stenotrophomonas maltophilia SKK35 and RA8 Genome sequencing: Analysis and
RT Comparison of Viurlence genes.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
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:CCP18613.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CALM01001212; CCP18613.1; -; Genomic_DNA.
DR RefSeq; WP_006397175.1; NZ_CALM01001212.1.
DR AlphaFoldDB; M5D3B3; -.
DR Proteomes; UP000012177; Unassembled WGS sequence.
DR GO; GO:0003864; F:3-methyl-2-oxobutanoate hydroxymethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016833; F:oxo-acid-lyase activity; IEA:UniProt.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 6.10.250.2750; -; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR42905:SF16; CARBOXYPHOSPHONOENOLPYRUVATE PHOSPHONOMUTASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_5G07230); 1.
DR PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR Pfam; PF13714; PEP_mutase; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000313|EMBL:CCP18613.1};
KW Transferase {ECO:0000313|EMBL:CCP18613.1}.
SQ SEQUENCE 276 AA; 28601 MW; D7B273463E3237A7 CRC64;
MTSPDADTRR KRATFRQLHA QGCFVLPNPW DVGSARYLQR QGFQALATTS AGCAWSEGRP
DGAVSLQATL EHLRLMVAAT PLPLNADFGD GFGATPGAVE EAVAAAIDTG VAALSIEDAS
GVADAPLRPI DEAVQRLRAA RAAIDRAGGE VLLVGRAENF FVGVPDLQDA LQRLRAYAEA
GADVLYAPGI TTREQISAVV AAAGSKPVNL LVGGPTPLSL QDIAALGVRR VSLGGALARA
AWGGLMQATQ PIVQDGRFDG LQQAASGAAL NALFRR
//