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Database: UniProt
Entry: L0IMU6_THETR
LinkDB: L0IMU6_THETR
Original site: L0IMU6_THETR 
ID   L0IMU6_THETR            Unreviewed;       367 AA.
AC   L0IMU6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Aminomethyltransferase {ECO:0000256|ARBA:ARBA00012616, ECO:0000256|HAMAP-Rule:MF_00259};
DE            EC=2.1.2.10 {ECO:0000256|ARBA:ARBA00012616, ECO:0000256|HAMAP-Rule:MF_00259};
DE   AltName: Full=Glycine cleavage system T protein {ECO:0000256|ARBA:ARBA00031395, ECO:0000256|HAMAP-Rule:MF_00259};
GN   Name=gcvT {ECO:0000256|HAMAP-Rule:MF_00259};
GN   ORFNames=Thethe_01958 {ECO:0000313|EMBL:AGB19566.1};
OS   Thermoanaerobacterium thermosaccharolyticum M0795.
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacterium.
OX   NCBI_TaxID=698948 {ECO:0000313|EMBL:AGB19566.1, ECO:0000313|Proteomes:UP000010845};
RN   [1] {ECO:0000313|EMBL:AGB19566.1, ECO:0000313|Proteomes:UP000010845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M0795 {ECO:0000313|EMBL:AGB19566.1,
RC   ECO:0000313|Proteomes:UP000010845};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Feinberg L., Folden J., Hogsett D.,
RA   Shaw J., Woyke T.;
RT   "Complete sequence of chromosome of Thermoanaerobacterium
RT   thermosaccharolyticum M0795.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. {ECO:0000256|HAMAP-Rule:MF_00259}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_00259};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. {ECO:0000256|HAMAP-Rule:MF_00259}.
CC   -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000256|ARBA:ARBA00008609,
CC       ECO:0000256|HAMAP-Rule:MF_00259}.
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DR   EMBL; CP003066; AGB19566.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0IMU6; -.
DR   KEGG; tto:Thethe_01958; -.
DR   PATRIC; fig|698948.3.peg.1956; -.
DR   HOGENOM; CLU_007884_10_2_9; -.
DR   Proteomes; UP000010845; Chromosome.
DR   GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
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   HAMAP; MF_00259; GcvT; 1.
DR   InterPro; IPR006223; GCS_T.
DR   InterPro; IPR022903; GCS_T_bac.
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, ECO:0000256|HAMAP-
KW   Rule:MF_00259};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00259}.
FT   DOMAIN          10..260
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          284..362
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   367 AA;  41287 MW;  FB9EEE1AC184D987 CRC64;
     MDNNLKKTPL YDTHLKYGAK MIDFAGFSMP VQYESILKEH EAVRKSAGLF DVSHMGEIII
     EGKDSEKFIN YIISNNIAKI SDNQAMYSPM CYANGTTVDD LLVYKFSNEK YMLVVNASNI
     DKDYNWIIEN KSGYNIAVKN ISNEVSELAL QGPKAQEILQ KMTEYNLDDM KYYHFDKINL
     AGVSCLISRS GYTGEDGFEI FLKNVDAQSM WEKILAVGEE FGIKPAGLGA RDTLRFEAGL
     PLYGNELSDE ITPLEAGLGS FVKFEKDFIG RDALFKQKQD GLKRKIVGFE MIENGIPRHG
     YDVCAQGEKI GYVTTGYLSP TLKKNIGMAL ISSKFANIGN EISIIIRNKP LKAIVTSKNF
     YKKNYKK
//
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