ID I3LIR4_PIG Unreviewed; 403 AA.
AC I3LIR4; A0A4X1SUG2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 73.
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=AMT {ECO:0000313|Ensembl:ENSSSCP00000023970.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000023970.1, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000023970.1, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000023970.1,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HDB10299.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000023970.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. {ECO:0000256|ARBA:ARBA00003631,
CC ECO:0000256|RuleBase:RU003981}.
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:0000256|ARBA:ARBA00043710,
CC ECO:0000256|RuleBase:RU003981};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|ARBA:ARBA00011690,
CC ECO:0000256|RuleBase:RU003981}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|RuleBase:RU003981}.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000256|ARBA:ARBA00008609,
CC ECO:0000256|RuleBase:RU003981}.
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DR EMBL; DQIR01154822; HDB10299.1; -; Transcribed_RNA.
DR RefSeq; NP_001231355.1; NM_001244426.1.
DR STRING; 9823.ENSSSCP00000023970; -.
DR PaxDb; 9823-ENSSSCP00000023970; -.
DR Ensembl; ENSSSCT00000031431.4; ENSSSCP00000023970.1; ENSSSCG00000022975.4.
DR Ensembl; ENSSSCT00005071666.1; ENSSSCP00005044705.1; ENSSSCG00005044448.1.
DR GeneID; 396679; -.
DR KEGG; ssc:396679; -.
DR CTD; 275; -.
DR eggNOG; KOG2770; Eukaryota.
DR GeneTree; ENSGT00940000157524; -.
DR HOGENOM; CLU_007884_10_0_1; -.
DR OMA; MPVQYPA; -.
DR OrthoDB; 5473523at2759; -.
DR TreeFam; TF313026; -.
DR Reactome; R-SSC-6783984; Glycine degradation.
DR Proteomes; UP000008227; Chromosome 13.
DR Bgee; ENSSSCG00000022975; Expressed in hindlimb bud and 32 other cell types or tissues.
DR Genevisible; I3LIR4; SS.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:Ensembl.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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 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 NCBIfam; TIGR00528; gcvT; 1.
DR PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR43757:SF15; 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 1: Evidence at protein level;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000256|RuleBase:RU003981};
KW Methyltransferase {ECO:0000313|EMBL:HDB10299.1};
KW Mitochondrion {ECO:0000256|RuleBase:RU003981};
KW Proteomics identification {ECO:0007829|PeptideAtlas:I3LIR4};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003981};
KW Transit peptide {ECO:0000256|RuleBase:RU003981}.
FT DOMAIN 38..291
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 318..395
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 403 AA; 43782 MW; E595761A07F1B6CD CRC64;
MQRTVSMVSR MGLRLQALPL SLGRPLSCAQ DVLRRTPLYD FHLAHGGKMV AFAGWSLPVQ
YRDSHVDSHL HTRQHCSLFD VSHMLQTKIF GSDRVKMMES LVVGDIAELK PNQGTLSLFT
NEAGGILDDL IVTNTSEGHL YVVSNAGCRE KDLTLMQDRV RELQNTGGDI GLEVMDNALL
ALQGPTAAQV LQAGVTDDLR KLPFMTSAVM EVFGVSGCRV TRCGYTGEDG VEISVPAAEA
VRLATALLEN PEVKLAGLAA RDSLRLEAGL CLYGNDIDEH TTPVEGSLSW TLGKRRRAAM
DFPGASVIVP QLKSKVQRRR VGLTCEGAPV RAHSPILSTE GTVIGTVTSG CPSPCLKKNV
AMGYVPYEHS RPGTLLLVEV RRKQQVAVVS KMPFVPTSYY TLK
//
