ID   GCST_PYRFU              Reviewed;         398 AA.
AC   Q8U185;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=PF1341;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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; AE009950; AAL81465.1; -; Genomic_DNA.
DR   RefSeq; WP_011012487.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U185; -.
DR   SMR; Q8U185; -.
DR   STRING; 186497.PF1341; -.
DR   PRIDE; Q8U185; -.
DR   EnsemblBacteria; AAL81465; AAL81465; PF1341.
DR   GeneID; 41713144; -.
DR   KEGG; pfu:PF1341; -.
DR   PATRIC; fig|186497.12.peg.1404; -.
DR   eggNOG; arCOG00756; Archaea.
DR   HOGENOM; CLU_007884_10_2_2; -.
DR   OMA; MPVQYPA; -.
DR   OrthoDB; 25548at2157; -.
DR   PhylomeDB; Q8U185; -.
DR   Proteomes; UP000001013; 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_0000122624"
SQ   SEQUENCE   398 AA;  45711 MW;  8047112633FC4826 CRC64;
     MAKRVHLFDW HKEHAKKIEE FAGWEMPIWY SSIKEEHLAV RNAVGVFDVS HMGEILFKGK
     DALKFLQYTT TNDISKPPAI SGTYTLVLNE RGAIKDETLV FNMGNNEYLM ICDADAFEKL
     YAWFTYLKKT IEQFTKLDLE IELKTYDIAM FAVQGPKARD LAMDLFGIDI NEMWWFQGRW
     VELDGIKMLL SRSGYTGENG FEVYIEDLNP YHPDEEKRGK PEKALHVWER ILEEGQKYGI
     KPAGLGARDT LRLEAGYTLY GNDTKELQLL STDIDEVTPL QANLEFAIYW DKDFIGKDAL
     LKQKEKGLGR KLVHFKMLEK SVPREGYKVY ANGELIGEVT SGTLSPLLNI GIGIAFVKEE
     YAKPGVEIEI DIRGTRKKAI TVTPPFYDPK KYGLFREE