ID A0A0M9A9S2_9HYME Unreviewed; 641 AA.
AC A0A0M9A9S2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Aminomethyltransferase, mitochondrial {ECO:0000256|ARBA:ARBA00015825};
DE EC=2.1.2.10 {ECO:0000256|ARBA:ARBA00012616};
DE AltName: Full=Glycine cleavage system T protein {ECO:0000256|ARBA:ARBA00031395};
GN ORFNames=WN51_02661 {ECO:0000313|EMBL:KOX79396.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX79396.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX79396.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX79396.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX79396.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. {ECO:0000256|ARBA:ARBA00003631}.
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 -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|ARBA:ARBA00011690}.
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; KQ435711; KOX79396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9A9S2; -.
DR STRING; 166423.A0A0M9A9S2; -.
DR OrthoDB; 5473523at2759; -.
DR Proteomes; UP000053105; Unassembled WGS sequence.
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:0006546; P:glycine catabolic process; IEA:InterPro.
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 SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR SUPFAM; SSF103025; Folate-binding domain; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW Methyltransferase {ECO:0000313|EMBL:KOX79396.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053105};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KOX79396.1}.
FT DOMAIN 210..464
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 492..571
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
FT REGION 119..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 641 AA; 70840 MW; 4758213F767C1C16 CRC64;
MKTANQPCVP ASFLKSKGDD VRPRRVLWFF LVQEPNADSA ELDRIDKNDK ALSSNSLVVR
LDDLSGTLAI STVSGQKEKS KRRDDQNFST NMLKLQQSSN VPGQLEAYFL ERSERKERVL
GSNESRKIRD RGLSSADAGA RDDGDEKGNV RLKVLKKKVQ QTTTTKKETT NANACLIDSE
TRSNETEGRR SSSTASVSTA PTPEPRKTCL HDLHVEYRGK IINFSGWLLP VQYQEAIAAS
HQHTRSFASL FDVGHMLQTQ ASGKDVTEFL ESLTTSDLRN LNRGSAVLTV FTNENGGILD
DLIITKDDDD RYFVVSNAAR RDEDTELLLQ QQENYKRRGK SVKLQFLDPL EQSLVALQGP
TAASVLRSII KINLTHLSFM NSVETTVFGN PVRVTRCGYT GEDGFEISMP AKIARTLAQA
ILDTPDTKLA GLGARDSLRL EAGLCLYGHD IDEETTPVEA GLTWLIAKRR REEANFPGAK
RILSQIKTGT VKKRIGLTVV HGPPVREGAC ILTPEGERVG KITSGGPSPT LGRSIAMGYV
PPELAHYGGG ILVEVRGKTY KATVTKMPFV KTNYYTAKKS NLKIPFLFIP KGLTYLSRKS
NLTTCCFLNL KKSNFKSNLT KLNNNLPNSK SSESGDYLDK E
//
