ID A9PL00_POPTM Unreviewed; 408 AA. AC A9PL00; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 11-DEC-2019, entry version 46. DE RecName: Full=Aminomethyltransferase {ECO:0000256|RuleBase:RU003981}; DE EC=2.1.2.10 {ECO:0000256|RuleBase:RU003981}; DE AltName: Full=Glycine cleavage system T protein {ECO:0000256|RuleBase:RU003981}; GN Name=gdcT1 {ECO:0000313|EMBL:ABO61732.1}; OS Populus tremuloides (Quaking aspen). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus. OX NCBI_TaxID=3693 {ECO:0000313|EMBL:ABO61732.1}; RN [1] {ECO:0000313|EMBL:ABO61732.1} RP NUCLEOTIDE SEQUENCE. RA Rajinikanth M., Harding S.A., Tsai C.-J.; RT "The Glycine Decarboxylase Complex Multienzyme Family in Populus."; RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of CC glycine. {ECO:0000256|RuleBase:RU003981}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)- CC aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene- CC 5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + CC NH4(+); Xref=Rhea:RHEA:16945, Rhea:RHEA-COMP:10475, Rhea:RHEA- CC COMP:10492, ChEBI:CHEBI:15636, ChEBI:CHEBI:28938, ChEBI:CHEBI:57453, CC ChEBI:CHEBI:83100, ChEBI:CHEBI:83143; EC=2.1.2.10; CC Evidence={ECO:0000256|RuleBase:RU003981}; CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P, CC T, L and H. {ECO:0000256|RuleBase:RU003981}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|RuleBase:RU003981}. CC -!- SIMILARITY: Belongs to the GcvT family. CC {ECO:0000256|RuleBase:RU003981}. 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; EF150633; ABO61732.1; -; mRNA. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro. DR Gene3D; 3.30.1360.120; -; 1. DR InterPro; IPR006223; GCS_T. 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 Pfam; PF01571; GCV_T; 1. DR Pfam; PF08669; GCV_T_C; 1. DR PIRSF; PIRSF006487; GcvT; 1. DR SUPFAM; SSF101790; SSF101790; 1. DR TIGRFAMs; TIGR00528; gcvT; 1. PE 2: Evidence at transcript level; KW Aminotransferase {ECO:0000256|RuleBase:RU003981}; KW Mitochondrion {ECO:0000256|RuleBase:RU003981}; KW Transferase {ECO:0000256|RuleBase:RU003981}; KW Transit peptide {ECO:0000256|RuleBase:RU003981}. FT DOMAIN 41..296 FT /note="GCV_T" FT /evidence="ECO:0000259|Pfam:PF01571" FT DOMAIN 324..400 FT /note="GCV_T_C" FT /evidence="ECO:0000259|Pfam:PF08669" FT REGION 328..348 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 408 AA; 44336 MW; 8B9123A288BA1FDB CRC64; MRGGGLWQLG LSITRRLAQT DKKAVGRRYF ASEAEMKKTV LYDFHVANGG KMVPFAGWSM PIQYKDSIME STVNCRQNGS LFDVSHMCGF SLKGKDCVPF LEKLVIADVA ALAPGTGTLT VFTNEKGGAI DDSVITKVTD DHMYIVVNAG CKDKDLAHIE AHMKSFKAKG GDVSWHIHDE RSLLALQGPL AAPVLQHLTK EDLSKVYFGE FRITDINGVR CFINRTGYTG EDGFEISVPS ENAVDLAKAT LEKSEGKVRL TGLGARDSLR LEAGLCLYGN DMEQHITPVE AGLNWAIGKR RKAEGGFLGA EVILKQLAEG PKIRLVGFSS TGPPPRSHSE IQDEKGTSIG EITSGGFSPC LKKNIAMGYV KSGFHKSGTK AKILVRGKAY DGVVTKKPFV PTKYYKPS //