ID GCST_RALPJ Reviewed; 375 AA. AC B2UG80; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 27-MAR-2024, entry version 98. DE RecName: Full=Aminomethyltransferase {ECO:0000255|HAMAP-Rule:MF_00259}; DE EC=2.1.2.10 {ECO:0000255|HAMAP-Rule:MF_00259}; DE AltName: Full=Glycine cleavage system T protein {ECO:0000255|HAMAP-Rule:MF_00259}; GN Name=gcvT {ECO:0000255|HAMAP-Rule:MF_00259}; GN OrderedLocusNames=Rpic_3487; OS Ralstonia pickettii (strain 12J). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=402626; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12J; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C., RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Marsh T., Richardson P.; RT "Complete sequence of chromosome 1 of Ralstonia pickettii 12J."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of CC glycine. {ECO:0000255|HAMAP-Rule:MF_00259}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + N(6)-[(R)-S(8)- CC aminomethyldihydrolipoyl]-L-lysyl-[protein] = (6R)-5,10- CC methylene-5,6,7,8-tetrahydrofolate + N(6)-[(R)-dihydrolipoyl]-L- CC lysyl-[protein] + NH4(+); Xref=Rhea:RHEA:16945, Rhea:RHEA-COMP:10475, CC Rhea:RHEA-COMP:10492, ChEBI:CHEBI:15636, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:57453, ChEBI:CHEBI:83100, ChEBI:CHEBI:83143; EC=2.1.2.10; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00259}; CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P, CC T, L and H. {ECO:0000255|HAMAP-Rule:MF_00259}. CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000255|HAMAP- CC Rule:MF_00259}. 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; CP001068; ACD28607.1; -; Genomic_DNA. DR AlphaFoldDB; B2UG80; -. DR SMR; B2UG80; -. DR STRING; 402626.Rpic_3487; -. DR KEGG; rpi:Rpic_3487; -. DR eggNOG; COG0404; Bacteria. DR HOGENOM; CLU_007884_10_2_4; -. DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule. DR Gene3D; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1. DR Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1. DR Gene3D; 4.10.1250.10; Aminomethyltransferase fragment; 1. DR HAMAP; MF_00259; GcvT; 1. DR InterPro; IPR006223; GCS_T. DR InterPro; IPR022903; GCS_T_bac. DR InterPro; IPR028896; GCST/YgfZ/DmdA. DR InterPro; IPR013977; GCV_T_C. DR InterPro; IPR006222; GCV_T_N. DR InterPro; IPR029043; GcvT/YgfZ_C. DR InterPro; IPR027266; TrmE/GcvT_dom1. DR NCBIfam; TIGR00528; gcvT; 1. DR PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1. DR PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 1. DR Pfam; PF01571; GCV_T; 1. DR Pfam; PF08669; GCV_T_C; 1. DR PIRSF; PIRSF006487; GcvT; 1. DR SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1. DR SUPFAM; SSF103025; Folate-binding domain; 1. PE 3: Inferred from homology; KW Aminotransferase; Transferase. FT CHAIN 1..375 FT /note="Aminomethyltransferase" FT /id="PRO_1000114108" SQ SEQUENCE 375 AA; 40148 MW; 6E8CAE7C9F89D7CA CRC64; MTLQHTPLNA IHRSLGARMV DFGGWDMPVN YGSQIEEHHA VRQDAGVFDV SHMCVVDLTG ARVRDFLRGL LANNVDKLQT PGKALYSCML NPKGGVIDDL IVYFFREDWF RLVVNAGTAP TDLEWIVAQN AAAGTDVTIT PRRSDNNAGA EPLGILAVQG PNARAKTYAA LPGSQAVGDA LKPFNAGFVT VENVGEIMVA RTGYTGEDGF ELVVPAAQIA GVWERLLQAG VRPAGLGARD TLRLEAGMNL YGQDMDEHVS PLDAGLAWTV DLQSERDFTG KAALQAGGQR EQFVGLILRD KGGVLRAHQK VITAAGDGEI TSGTFSPSLS LSIALARLPK EVPVGTDVQV EIRDRKLTAT VVKLPFVRNG KALVS //