ID A0A0J8D425_CLOCY Unreviewed; 371 AA.
AC A0A0J8D425;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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 ECO:0000313|EMBL:KMT20930.1};
GN ORFNames=CLCY_1c01640 {ECO:0000313|EMBL:KMT20930.1};
OS Clostridium cylindrosporum DSM 605.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121307 {ECO:0000313|EMBL:KMT20930.1, ECO:0000313|Proteomes:UP000036756};
RN [1] {ECO:0000313|EMBL:KMT20930.1, ECO:0000313|Proteomes:UP000036756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 605 {ECO:0000313|EMBL:KMT20930.1,
RC ECO:0000313|Proteomes:UP000036756};
RA Poehlein A., Schiel-Bengelsdorf B., Bengelsdorf F., Daniel R., Duerre P.;
RT "Draft genome sequence of the purine-degrading Clostridium cylindrosporum
RT HC-1 (DSM 605).";
RL Submitted (JUN-2015) 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}.
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:KMT20930.1}.
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DR EMBL; LFVU01000028; KMT20930.1; -; Genomic_DNA.
DR RefSeq; WP_048571328.1; NZ_LFVU01000028.1.
DR AlphaFoldDB; A0A0J8D425; -.
DR STRING; 1121307.CLCY_1c01640; -.
DR PATRIC; fig|1121307.3.peg.525; -.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000036756; Unassembled WGS sequence.
DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
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 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}; Methyltransferase {ECO:0000313|EMBL:KMT20930.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036756};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00259}.
FT DOMAIN 9..260
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 285..362
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 371 AA; 40929 MW; E834CDA9FD5B02CC CRC64;
MSNLKKTPLF DAHQKVGGKI VEFAGWEMPI QYEGLVEEHT AVRTQAGIFD VSHMGEVDIT
GPDAQKFVDY LVTNDIAGLE NTQIAYNLMC NENGGIVDDL LVYKYDENHM YLVINAANID
KDVKWIEEKA KGFDVKVENV SPEVAEIAIQ GPEAQAILQK VSDVDLSTIK FFYFNDSVNV
AGVKCLVSRT GYTGEDGFEV YTTNDAIEKV WNALLEAGAD VLKPAGLGAR DTLRFEAALP
LYGNEMSDTI SPLEAGLGFF VKLGKASDFI GKSVLVKQKE EGLKRKTIGF EMKERGIPRH
GYDVVKDGKV IGAVATGYFS PTLQKTIGTA LVEAEYAELG TEIEIQIRNK TAKAEVISKR
FYTKKTKQEK K
//
