ID GCST_ECOUT Reviewed; 364 AA. AC Q1R7C6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 16-JUN-2009, entry version 25. DE RecName: Full=Aminomethyltransferase; DE EC=2.1.2.10; DE AltName: Full=Glycine cleavage system T protein; GN Name=gcvT; OrderedLocusNames=UTI89_C3290; OS Escherichia coli (strain UTI89 / UPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=364106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16585510; DOI=10.1073/pnas.0600938103; RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., RA Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., RA Hultgren S.J., Gordon J.I.; RT "Identification of genes subject to positive selection in RT uropathogenic strains of Escherichia coli: a comparative genomics RT approach."; RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(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; CP000243; ABE08738.1; -; Genomic_DNA. DR RefSeq; YP_542269.1; -. DR SMR; Q1R7C6; 4-364. DR GeneID; 3990521; -. DR GenomeReviews; CP000243_GR; UTI89_C3290. DR KEGG; eci:UTI89_C3290; -. DR HOGENOM; Q1R7C6; -. DR OMA; Q1R7C6; VEIRGKW. DR BioCyc; ECOL364106:UTI89_C3290-MON; -. 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 1 364 Aminomethyltransferase. FT /FTId=PRO_1000047662. SQ SEQUENCE 364 AA; 40149 MW; F54BFBB25282F43A CRC64; MAQQTPLYEQ HTLCGARMVD FHGWMMPLHY GSQIDEHHAV RTDAGMFDVS HMTIVDLRGS RTREFLRYLL ANDVAKLTKS GKALYSGMLN ASGGVIDDLI VYYFTEDFFR LVVNSATREK DLSWITQHAE PFGIEITVRD DLSMIAVQGP NAQAKAATLF NDAQRQAVEG MKPFFGVQAG DLFIATTGYT GEAGYEIALP NEKAADFWRA LVEAGVKPCG LGARDTLRLE AGMNLYSQEM DETISPLAAN MGWTIAWEPA DRDFIGREAL EAQREHGTEK LVGLVMTEKG VLRNELPVRF TDAQGNQHEG IITSGTFSPT LGYSIALARV PEGIGETAIV QIRNREMPVK VTKPVFVRNG KAVA //