ID GCST_CORJK Reviewed; 389 AA. AC Q4JXU5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 16-JUN-2009, entry version 36. DE RecName: Full=Aminomethyltransferase; DE EC=2.1.2.10; DE AltName: Full=Glycine cleavage system T protein; GN Name=gcvT; OrderedLocusNames=jk0210; OS Corynebacterium jeikeium (strain K411). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=306537; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005; RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., RA Albersmeier A., Bekel T., Bischoff N., Brune I., Chakraborty T., RA Kalinowski J., Meyer F., Rupp O., Schneiker S., Viehoever P., RA Puehler A.; RT "Complete genome sequence and analysis of the multiresistant RT nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring RT bacterium of the human skin flora."; RL J. Bacteriol. 187:4671-4682(2005). 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; CR931997; CAI36362.1; -; Genomic_DNA. DR RefSeq; YP_249980.1; -. DR GeneID; 3433828; -. DR GenomeReviews; CR931997_GR; jk0210. DR KEGG; cjk:jk0210; -. DR NMPDR; fig|306537.3.peg.519; -. DR HOGENOM; Q4JXU5; -. DR OMA; Q4JXU5; VEIRGKW. DR BioCyc; CJEI306537:JK0210-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 1 389 Aminomethyltransferase. FT /FTId=PRO_1000047660. SQ SEQUENCE 389 AA; 40653 MW; EB6B4466CF614591 CRC64; MTELKKTALH LVHEKLGARF TDFGGWDMPL KYSSELDEHH AVRNAVGVFD LSHMGEVRVT GPQAAEFLDH ALISKLSAVK VGKAKYSMIC TESGGIIDDL ITYRLGDNEF LIVPNAGNVD NVVSALQGRT EGFDVEVNNE SDATSMIAVQ GPKAAQAMLE IVENVVDAPE ASGAGETVAE AIEGLGYYAA FSGVAAGQPV LVARTGYTGE DGFELIVAND GAETVWTKAM DQAAQLGGLP CGLACRDTLR LEAGMPLYGN ELSLKLTPVD AGLGILAATK SKDSFVGRDA IVSAKEKGTQ QVLIGLAGEG RRAARGGYEV FAGDGEKAIG AVTSGALSPT LGHPVALAYV AKSAVSSGAA AEGATVEVDI RGKRFEYKVV ALPFYSREK //