GCST_THEGJ
ID GCST_THEGJ Reviewed; 398 AA.
AC C5A3P0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=TGAM_0350;
OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=593117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT the most radioresistant organism known amongst the Archaea.";
RL Genome Biol. 10:R70.1-R70.23(2007).
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; CP001398; ACS32852.1; -; Genomic_DNA.
DR RefSeq; WP_015857970.1; NC_012804.1.
DR AlphaFoldDB; C5A3P0; -.
DR SMR; C5A3P0; -.
DR STRING; 593117.TGAM_0350; -.
DR PaxDb; C5A3P0; -.
DR EnsemblBacteria; ACS32852; ACS32852; TGAM_0350.
DR GeneID; 7987816; -.
DR KEGG; tga:TGAM_0350; -.
DR PATRIC; fig|593117.10.peg.348; -.
DR eggNOG; arCOG00756; Archaea.
DR HOGENOM; CLU_007884_10_2_2; -.
DR OMA; MPVQYPA; -.
DR OrthoDB; 25548at2157; -.
DR Proteomes; UP000001488; 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_1000204643"
SQ SEQUENCE 398 AA; 45407 MW; F07877641DA422F9 CRC64;
MVKRVHIFDW HKEHAKKVEE FAGWEMPIWY SSIKEEHLAV RNGVGIFDVS HMGEFIFRGK
DALEFLQYVT TNDISKPPAI SGTYTLVLNE RGAVKDETLV FNLGNDTYMM VCDSDAFEKL
EAWFNAIKRG IEKFGSIDLE IENKTYDMAM FSVQGPKARD LAKDLFGIDI NDLWWFQAKE
VELDGIKMLL SRSGYTGENG WEVYFEDKNP YHPNPEKRGR PEKALHVWER ILEEGEKYGI
KPAGLGARDT LRLEAGYTLY GNETKELQLL STDIDEVTPL QANLDFAIFW DKEFIGKEAL
LKQKERGLGR KMVHFKMVDR GIPREGYKVL ANGEVIGEVT SGTLSPLLGI GIGIAFVKEE
YAKPGLEIEV EIRGKPKRAV TVSPPFYDPK KYGAFREE
