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Database: UniProt
Entry: G2ZMQ5_9RALS
LinkDB: G2ZMQ5_9RALS
Original site: G2ZMQ5_9RALS 
ID   G2ZMQ5_9RALS            Unreviewed;       375 AA.
AC   G2ZMQ5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
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:CCA80318.1};
GN   ORFNames=BDB_90016 {ECO:0000313|EMBL:CCA80318.1};
OS   blood disease bacterium R229.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=741978 {ECO:0000313|EMBL:CCA80318.1};
RN   [1] {ECO:0000313|EMBL:CCA80318.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R229 {ECO:0000313|EMBL:CCA80318.1};
RX   PubMed=21931687; DOI=10.1371/journal.pone.0024356;
RA   Remenant B., de Cambiaire J.C., Cellier G., Jacobs J.M., Mangenot S.,
RA   Barbe V., Lajus A., Vallenet D., Medigue C., Fegan M., Allen C., Prior P.;
RT   "Ralstonia syzygii, the Blood Disease Bacterium and some Asian R.
RT   solanacearum strains form a single genomic species despite divergent
RT   lifestyles.";
RL   PLoS ONE 6:e24356-e24356(2011).
RN   [2] {ECO:0000313|EMBL:CCA80318.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R229 {ECO:0000313|EMBL:CCA80318.1};
RA   Genoscope - CEA;
RL   Submitted (APR-2011) 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; FR854065; CCA80318.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2ZMQ5; -.
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:CCA80318.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00259}.
FT   DOMAIN          8..269
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          292..367
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   375 AA;  40161 MW;  6976F46B70C1B562 CRC64;
     MTLQHTPLNA IHRSLGARMV DFGGWDMPVN YGSQIEEHHA VRRDAGIFDV SHMCVVDLTG
     ARVRDFLRGL LANNVDKLQA PGKALYTCML NPKGGVIDDL IVYFFREDWF RLVVNAGTAP
     TDIEWIVAQN AAAGTGVTIT PRRSDNNTGT EPLGILAVQG PNARAKTYAA LPGTQAVGEA
     LKPFNAGFAT LDGVGEIMVA RTGYTGEDGF ELVVPAAQIA GVWERLLQAG VHPCGLGARD
     TLRLEAGMNL YGQDMDEHVS PLDAGLAWTV DLQSERDFNG KATLAANGQR DQFVGLLLRD
     KGGVLRAHQK VITPAGDGEI TSGTFSPSLS QSIALARLPK DVAIGTDVLV EIRDRKLTAT
     VVKLPFVRNG KALVS
//
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