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Database: UniProt
Entry: A0A2T4AK38_TRIHA
LinkDB: A0A2T4AK38_TRIHA
Original site: A0A2T4AK38_TRIHA 
ID   A0A2T4AK38_TRIHA        Unreviewed;       437 AA.
AC   A0A2T4AK38;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Aminomethyltransferase {ECO:0000256|ARBA:ARBA00012616, ECO:0000256|RuleBase:RU003981};
DE            EC=2.1.2.10 {ECO:0000256|ARBA:ARBA00012616, ECO:0000256|RuleBase:RU003981};
DE   AltName: Full=Glycine cleavage system T protein {ECO:0000256|ARBA:ARBA00031395, ECO:0000256|RuleBase:RU003981};
GN   ORFNames=M431DRAFT_479059 {ECO:0000313|EMBL:PTB57450.1};
OS   Trichoderma harzianum CBS 226.95.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=983964 {ECO:0000313|EMBL:PTB57450.1, ECO:0000313|Proteomes:UP000241690};
RN   [1] {ECO:0000313|EMBL:PTB57450.1, ECO:0000313|Proteomes:UP000241690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 226.95 {ECO:0000313|EMBL:PTB57450.1,
RC   ECO:0000313|Proteomes:UP000241690};
RG   DOE Joint Genome Institute;
RA   Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA   Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA   Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT   "Multiple horizontal gene transfer events from other fungi enriched the
RT   ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT   plant biomass.";
RL   Submitted (JUL-2016) 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 + 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|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; KZ679677; PTB57450.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4AK38; -.
DR   STRING; 983964.A0A2T4AK38; -.
DR   OrthoDB; 5473523at2759; -.
DR   Proteomes; UP000241690; Unassembled WGS sequence.
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; 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: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 {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000256|RuleBase:RU003981};
KW   Mitochondrion {ECO:0000256|RuleBase:RU003981};
KW   Reference proteome {ECO:0000313|Proteomes:UP000241690};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003981};
KW   Transit peptide {ECO:0000256|RuleBase:RU003981}.
FT   DOMAIN          50..318
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          352..427
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   437 AA;  46684 MW;  EAA398F03940CFBF CRC64;
     MMKSFTRIAR ASPRVKASAS LSAAGRLSTA GSIRCASNAS SGEPLKKTPL YDFHVANGAK
     MVPFAGYHMP VQYSSLSLAD SHHFTRNHAS LFDVSHMVQH IFKGPAAAAF LEKVTPSSWS
     NVAPMSGKLT TFLWPGTGGI VDDTIVTRIG EDEFYVVTNG ACLDKDTKYI DEELGKFGGD
     VKWTRLDGSG LVALQGPQAA EILSEVLATD INLKEFYFGN TVQAELKLAD GGKTHPVLIS
     RGGYTGEDGF EISFNGKLYP ALESTVKAVE SLIKTAGPER LQMAGLGARD SLRLEAGMCL
     YGHDLDDTTT PVEAGLSWII SPERRKAGGF HGAEIILPQL TPKSKGGSGV ERRRVGFVVQ
     GAPAREGAEI QKDGQTIGTI TSGVPSPTLG KNIAMGYIKD GQHKAGTEVD VVVRGRKRQA
     VVTKMPFTPA KYWKAPA
//
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