ID   GCST_AERPE              Reviewed;         375 AA.
AC   Q9YBA2;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   05-MAY-2009, entry version 51.
DE   RecName: Full=Probable aminomethyltransferase;
DE            EC=2.1.2.10;
DE   AltName: Full=Glycine cleavage system T protein;
GN   Name=gcvT; OrderedLocusNames=APE_1695.1;
OS   Aeropyrum pernix.
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=56636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K1;
RX   MEDLINE=99310339; PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y.,
RA   Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H.,
RA   Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H.,
RA   Takamiya M., Masuda S., Funahashi T., Tanaka T., Kudoh Y.,
RA   Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y.,
RA   Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic
RT   crenarchaeon, Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine (By similarity).
CC   -!- CATALYTIC ACTIVITY: [Protein]-S(8)-aminomethyldihydrolipoyllysine
CC       + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-
CC       methylenetetrahydrofolate + NH(3).
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins:
CC       P, T, L and H (By similarity).
CC   -!- SIMILARITY: Belongs to the gcvT family.
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DR   EMBL; BA000002; BAA80696.2; -; Genomic_DNA.
DR   PIR; C72551; C72551.
DR   RefSeq; NP_148104.2; -.
DR   GeneID; 1446178; -.
DR   GenomeReviews; BA000002_GR; APE_1695.1.
DR   KEGG; ape:APE_1695.1; -.
DR   NMPDR; fig|272557.1.peg.1212; -.
DR   HOGENOM; Q9YBA2; -.
DR   OMA; Q9YBA2; HAREASW.
DR   BRENDA; 2.1.2.10; 256344.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004047; F:aminomethyltransferase activity; IEA:HAMAP.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavag...; IEA:HAMAP.
DR   HAMAP; MF_00259; -; 1.
DR   InterPro; IPR013977; GCV_T_C.
DR   InterPro; IPR006222; GCV_T_N.
DR   InterPro; IPR006223; GcvT.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   PIRSF; PIRSF006487; GcvT; 1.
DR   TIGRFAMs; TIGR00528; gcvT; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Complete proteome; Transferase.
FT   CHAIN         1    375       Probable aminomethyltransferase.
FT                                /FTId=PRO_0000122620.
SQ   SEQUENCE   375 AA;  41261 MW;  A1F809E5FA785EA9 CRC64;
     MPVRRHILED LHRSLGATFG EFAGWSVPMS YEGTLKEHMA VRREAGIFDI SHMGRMIVSG
     EGATELLERI YTKRVSKTKV GFMSGPTLAL NEYARVKDDE MPYRLGEEEW LIVPNAAVAD
     AMLEYFSSIA SSMGLNVSIR DLRERYALLA LQGPGAARVM EEMGGGDLLD LKPLQFRENA
     GIAGVTAYIV SRSGWTGEDG FEIIAEVEAA KRIFKAAVEA GAKPAGIAAR DTLRIEAGFV
     LGGHEYGEDP LRWPCAVSLR YGLGAIDWGK KGFVGEAALR ACRREGVRWI RVGLVMKKKY
     ARMIPRSGYR LYVDDVDVGW VTSGTFSPVI GRGVAQAYID SRYAYIGDTI EVDVRGKRGE
     ARLQEFPLVP LGSRG
//