ID GCST_SYNS9 Reviewed; 365 AA.
AC Q3AVT0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=Aminomethyltransferase {ECO:0000255|HAMAP-Rule:MF_00259};
DE EC=2.1.2.10 {ECO:0000255|HAMAP-Rule:MF_00259};
DE AltName: Full=Glycine cleavage system T protein {ECO:0000255|HAMAP-Rule:MF_00259};
GN Name=gcvT {ECO:0000255|HAMAP-Rule:MF_00259};
GN OrderedLocusNames=Syncc9902_2232;
OS Synechococcus sp. (strain CC9902).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=316279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9902;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9902.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. {ECO:0000255|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-methylene-
CC 5,6,7,8-tetrahydrofolate + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein]
CC + NH4(+); Xref=Rhea:RHEA:16945, Rhea:RHEA-COMP:10475, Rhea:RHEA-
CC COMP:10492, ChEBI:CHEBI:15636, ChEBI:CHEBI:28938, ChEBI:CHEBI:57453,
CC ChEBI:CHEBI:83100, ChEBI:CHEBI:83143; EC=2.1.2.10;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00259};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000255|HAMAP-Rule:MF_00259}.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000255|HAMAP-
CC Rule:MF_00259}.
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DR EMBL; CP000097; ABB27190.1; -; Genomic_DNA.
DR RefSeq; WP_011360967.1; NC_007513.1.
DR AlphaFoldDB; Q3AVT0; -.
DR SMR; Q3AVT0; -.
DR STRING; 316279.Syncc9902_2232; -.
DR KEGG; sye:Syncc9902_2232; -.
DR eggNOG; COG0404; Bacteria.
DR HOGENOM; CLU_007884_10_2_3; -.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000002712; 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; Transferase.
FT CHAIN 1..365
FT /note="Aminomethyltransferase"
FT /id="PRO_1000047723"
SQ SEQUENCE 365 AA; 39520 MW; B3EF05D83E47110D CRC64;
MLRTPLYELC RTGGGRMVPF AGWEMPVQFS GLIQEHKAVR NSVGMFDISH MGVLRLEGAN
PKDTLQQLVP SDLHRIGPGE ACYTVLLNDQ GGIRDDLIIY DLGAIDEKRG ALVLVINAAC
ADSDTAWIRE RMEPAGLTVT DIKNNGVLLA LQGPQAIPLL EQLSGEDLSG LPRFGHRDLQ
IQGLSNSVFT ARTGYTGEDG AELLLTAEDG QLLWSQLLEK GVAPCGLGAR DTLRLEAAMH
LYGQDMNADT NPFEAGLGWL VHLEMPADFI GRQALERAAE TGPNKRLVGL KLEGRAIARH
DYPVLHNGEP VGVVTSGTWS PTLEEPIALA SIPTALAKLG TNLSVEIRGK AQPATVVRRP
FYKRP
//
