GCST_DICDI
ID GCST_DICDI Reviewed; 403 AA.
AC Q54DD3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Aminomethyltransferase, mitochondrial;
DE EC=2.1.2.10;
DE AltName: Full=Glycine cleavage system T protein;
DE Short=GCVT;
DE Flags: Precursor;
GN Name=gcvT; ORFNames=DDB_G0292326;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. {ECO:0000250}.
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 -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000305}.
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DR EMBL; AAFI02000189; EAL61287.1; -; Genomic_DNA.
DR RefSeq; XP_629708.1; XM_629706.1.
DR AlphaFoldDB; Q54DD3; -.
DR SMR; Q54DD3; -.
DR STRING; 44689.DDB0231218; -.
DR PaxDb; Q54DD3; -.
DR PRIDE; Q54DD3; -.
DR EnsemblProtists; EAL61287; EAL61287; DDB_G0292326.
DR GeneID; 8628622; -.
DR KEGG; ddi:DDB_G0292326; -.
DR dictyBase; DDB_G0292326; gcvT.
DR eggNOG; KOG2770; Eukaryota.
DR HOGENOM; CLU_007884_10_0_1; -.
DR InParanoid; Q54DD3; -.
DR OMA; MPVQYPA; -.
DR PhylomeDB; Q54DD3; -.
DR Reactome; R-DDI-6783984; Glycine degradation.
DR PRO; PR:Q54DD3; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004047; F:aminomethyltransferase activity; IBA:GO_Central.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
DR Gene3D; 3.30.1360.120; -; 1.
DR InterPro; IPR006223; GCS_T.
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; Mitochondrion; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..403
FT /note="Aminomethyltransferase, mitochondrial"
FT /id="PRO_0000327652"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 403 AA; 44247 MW; AF126F821C858B45 CRC64;
MISQNIIKII QKSNKRYFSS SNELKKTALN ELHKELGAKM VPFCGWEMPV QYPAGVMKEH
LHVRKESGLF DVSHMGQLRI HGKDRVKFFE SIVVADLQAL PTGHSKLSVF TNEKGGIIDD
TMITNAGDSL YVVVNAGCAD KDISHINEKI KEFKSVNPTH DVSMQLLEDL SLIAIQGPTT
ESILQKFVKD QDITNMEFMT QRPMTIAGID CIVTRCGYTG EDGFEISVPS KQAVRLAELF
LATSNASIES GIKPAGLGAR DSLRLEAGLC LYGHDLNDDI TPIEASLNWL ISKRRREEGG
FPGASIIQKQ LQKDGCPQKR VGVIINGAPA REGCLILDPS TNQEIGKVTS GTISPITRQS
ISMAYVKTPF SKIGTQVNVS IRGKPITATI SKMPFVPTNY KKL
