GCST_THEON
ID GCST_THEON Reviewed; 398 AA.
AC B6YY21;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Probable 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}; OrderedLocusNames=TON_1494;
OS Thermococcus onnurineus (strain NA1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523850;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1;
RX PubMed=18790866; DOI=10.1128/jb.00746-08;
RA Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA Colwell R.R., Kim S.-J., Lee J.-H.;
RT "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT mixed heterotrophic and carboxydotrophic metabolism.";
RL J. Bacteriol. 190:7491-7499(2008).
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 + (R)-N(6)-(S(8)-
CC aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-
CC 5,6,7,8-tetrahydrofolate + (R)-N(6)-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; CP000855; ACJ16984.1; -; Genomic_DNA.
DR RefSeq; WP_012572456.1; NC_011529.1.
DR AlphaFoldDB; B6YY21; -.
DR SMR; B6YY21; -.
DR STRING; 523850.TON_1494; -.
DR PRIDE; B6YY21; -.
DR EnsemblBacteria; ACJ16984; ACJ16984; TON_1494.
DR GeneID; 7018529; -.
DR KEGG; ton:TON_1494; -.
DR PATRIC; fig|523850.10.peg.1506; -.
DR eggNOG; arCOG00756; Archaea.
DR HOGENOM; CLU_007884_10_2_2; -.
DR OMA; MPVQYPA; -.
DR OrthoDB; 25548at2157; -.
DR Proteomes; UP000002727; 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; 3.30.1360.120; -; 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 PANTHER; PTHR43757; PTHR43757; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR SUPFAM; SSF101790; SSF101790; 1.
DR TIGRFAMs; TIGR00528; gcvT; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Transferase.
FT CHAIN 1..398
FT /note="Probable aminomethyltransferase"
FT /id="PRO_1000114121"
SQ SEQUENCE 398 AA; 45239 MW; E75BC04E09ECABC2 CRC64;
MAKRVHIFDW HKKNAKKVEE FAGWEMPIWY SSIKDEHLAV RNGVAIFDVS HMGEFIFKGK
DALEFLQYVT TNDISKPPAI SGTYTLVLNE RGAVKDETLV FNMGNDTYMM VCDSDAFEKL
EAWFNAIKRG IEKFGELDLE IENKTYDMAM FSIQGPKARD LAKDLFDIDI NDLWWFQAKE
VELDGIKMLL SRSGYTGENG FEVYFEDANP YHPDPERRGE PEKALHVWKT ILEAGEKYGI
KPAGLGARDT LRLEAGYTLY GNETKELQLL STDIDEVTPL QANLDFAIFW DKEFIGKEAL
LKQRERGIPR KLVHFKMIDK GIPREGYKVY ANGELIGEVT SGTSSPLLGI GIGIAFVKTE
YAKPGVEIEV EIRGKPKKAV TVAPPFYDPK KYGAFREE
