ID A0A3M2SZQ1_9EURO Unreviewed; 453 AA.
AC A0A3M2SZQ1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 ORFNames=PHISP_06084 {ECO:0000313|EMBL:RMJ23051.1};
OS Aspergillus sp. HF37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1960876 {ECO:0000313|EMBL:RMJ23051.1, ECO:0000313|Proteomes:UP000272442};
RN [1] {ECO:0000313|EMBL:RMJ23051.1, ECO:0000313|Proteomes:UP000272442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HF37 {ECO:0000313|EMBL:RMJ23051.1,
RC ECO:0000313|Proteomes:UP000272442};
RA Tafer H., Lopandic K.;
RL Submitted (APR-2017) 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|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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RMJ23051.1}.
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DR EMBL; RAQS01000276; RMJ23051.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M2SZQ1; -.
DR STRING; 1960876.A0A3M2SZQ1; -.
DR Proteomes; UP000272442; 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; 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 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|RuleBase:RU003981};
KW Mitochondrion {ECO:0000256|RuleBase:RU003981};
KW Reference proteome {ECO:0000313|Proteomes:UP000272442};
KW Transferase {ECO:0000256|RuleBase:RU003981};
KW Transit peptide {ECO:0000256|RuleBase:RU003981}.
FT DOMAIN 68..344
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
SQ SEQUENCE 453 AA; 48706 MW; C7EB3CEDE817A80D CRC64;
MSAMRAMRRG ASLLGSRSVC LQSAPRLPGQ LRIPAARPLP QLFSRASVAQ PSVRFASSST
ESLSKTQLND LHMARGAKMV PFAGFSMPLQ YSDLSHVESH NWTREKASLF DVSHMVQHHL
SGPGALDLLM KVTPSSVDKL KPNTSTLSCL LEEVTGGIQD DSVITRRGED SFYFVTNAAR
REEDLAFLKA EIDAYRSANG ADSIKWDVLE DHALIALQGP LAPSALQSYI HPHGVSAADT
DLSTLYFGQC RSLHLTLPDG SPTPHPLLIS RTGYTGEDGF EISIPTAGSP ALPSQVAELL
VSKPDEVRLA GLAARDSLRL EAGMCLYGHD ITSAQTPPAG ALGWIIGKDR RELGTPQASF
NGASVILPQV ASPAKTLSQR RVGFTVEKGP PAREGAVIVD PADEQRTQIG VITSGLPGLH
KKGTEVGILV RNRVRKASVV GMPWVESKFY RPK
//
