ID GCST_BORA1 Reviewed; 366 AA. AC Q2KYM2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 16-JUN-2009, entry version 26. DE RecName: Full=Aminomethyltransferase; DE EC=2.1.2.10; DE AltName: Full=Glycine cleavage system T protein; GN Name=gcvT; OrderedLocusNames=BAV0491; OS Bordetella avium (strain 197N). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=360910; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16885469; DOI=10.1128/JB.01927-05; RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., RA King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., RA Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., RA Squares S., Woodward J., Parkhill J., Temple L.M.; RT "Comparison of the genome sequence of the poultry pathogen Bordetella RT avium with those of B. bronchiseptica, B. pertussis, and B. RT parapertussis reveals extensive diversity in surface structures RT associated with host interaction."; RL J. Bacteriol. 188:6002-6015(2006). CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of CC glycine (By similarity). CC -!- CATALYTIC ACTIVITY: [Protein]-S(8)-aminomethyldihydrolipoyllysine CC + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10- CC methylenetetrahydrofolate + NH(3). CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: CC P, T, L and H (By similarity). CC -!- SIMILARITY: Belongs to the gcvT family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM167904; CAJ48096.1; -; Genomic_DNA. DR RefSeq; YP_785024.1; -. DR GeneID; 6264780; -. DR GenomeReviews; AM167904_GR; BAV0491. DR KEGG; bav:BAV0491; -. DR NMPDR; fig|521.1.peg.1055; -. DR HOGENOM; Q2KYM2; -. DR OMA; Q2KYM2; VEIRGKW. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:HAMAP. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavag...; IEA:HAMAP. DR HAMAP; MF_00259; -; 1. DR InterPro; IPR013977; GCV_T_C. DR InterPro; IPR006222; GCV_T_N. DR InterPro; IPR006223; GcvT. DR Pfam; PF01571; GCV_T; 1. DR Pfam; PF08669; GCV_T_C; 1. DR PIRSF; PIRSF006487; GcvT; 1. DR TIGRFAMs; TIGR00528; gcvT; 1. PE 3: Inferred from homology; KW Aminotransferase; Complete proteome; Transferase. FT CHAIN 1 366 Aminomethyltransferase. FT /FTId=PRO_1000047647. SQ SEQUENCE 366 AA; 39328 MW; 9D0249FDC5E6BBBE CRC64; MSASLKHTPL AETHLAAGAR MVDFGGWEMP LAYGSQLEEH HAVRQDAGMF DVSHMLNADI TGPDATAFLR YLVANDVARL NTPGKALYSC MLNPQGGVID DLIIYYFAPD SWRVVVNAGT AEKDMAWMAR VAAAGNFDVV ITPRRDLAMI AVQGPNARAK VWAARPAWQP ASEGLGPFTA AILPEDTLVA RTGYTGEDGF EIVLPASAAV ALWQDLVAQG VRPCGLGARD TLRLEAGMNL YGQDMDELVQ PNQAGLSWTV SLKDAERRFI GRDALEQFAT PCAFLGLKLS ERGVMRAHMA VRTPQGMGLT TSGTMSPTLG VSIAFARLPL DVQPGSAVEV DIRGKWVPAL VCKLPFVRNG KAVEHS //