GCST_THEKO
ID GCST_THEKO Reviewed; 398 AA.
AC Q5JDG3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 97.
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=TK2035;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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; AP006878; BAD86224.1; -; Genomic_DNA.
DR RefSeq; WP_011250985.1; NC_006624.1.
DR AlphaFoldDB; Q5JDG3; -.
DR SMR; Q5JDG3; -.
DR STRING; 69014.TK2035; -.
DR EnsemblBacteria; BAD86224; BAD86224; TK2035.
DR GeneID; 3235069; -.
DR KEGG; tko:TK2035; -.
DR PATRIC; fig|69014.16.peg.1989; -.
DR eggNOG; arCOG00756; Archaea.
DR HOGENOM; CLU_007884_10_2_2; -.
DR InParanoid; Q5JDG3; -.
DR OMA; MPVQYPA; -.
DR OrthoDB; 25548at2157; -.
DR PhylomeDB; Q5JDG3; -.
DR Proteomes; UP000000536; 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; Reference proteome; Transferase.
FT CHAIN 1..398
FT /note="Probable aminomethyltransferase"
FT /id="PRO_0000122626"
SQ SEQUENCE 398 AA; 45136 MW; 6330AA2B35D2ABEB CRC64;
MVKRVHIFDW HKEHAKKVEE FAGWEMPIWY SSIKEEHLAV RNGVGIFDVS HMGEFIFRGK
DALEFLQYVT TNDISKPPAI SGTYTLVLNE RGAVKDETLV FNMGNDTYMM VCDSDAFEKL
DAWFNAIKRG IEKFGDIDLE IENKTYDMAM FSIQGPKARD LAKELFGIDI NDLWWFQAKE
VELDGIKMLL SRSGYTGENG FEVYFEDANP YHPDPSKRGE PEKALHVWKT ILEAGEKYGI
KPAGLGARDT LRLEAGYTLY GNETKEKQLL STDIDEVTPL QANLDFAIFW DKEFIGKEAL
LKQKERGLPS KMVHFKMVDK GVPREGYKVY KDGELIGEVT SGTLSPLLGI GIGIAFVKPE
YAVPGVEIEV EIRGKPKKAV TVAPPFYDPK KYGAFREE
