GCST_SCHPO
ID GCST_SCHPO Reviewed; 387 AA.
AC O14110; Q92364;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Probable aminomethyltransferase, mitochondrial;
DE EC=2.1.2.10;
DE AltName: Full=Glycine cleavage system T protein;
DE Short=GCVT;
DE Flags: Precursor;
GN Name=gcv1; ORFNames=n313, SPAC31G5.14;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Nagao K., Arioka M., Kadokura H., Yoda K., Yamasaki M.;
RT "The nucleotide sequence of a 9.1 kb DNA fragment of Schizosaccharomyces
RT pombe chromosome reveals the presence of pad1+/sks1+ gene and three
RT previously unknown open reading frames.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA12709.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D84656; BAA12709.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CU329670; CAB11698.1; -; Genomic_DNA.
DR PIR; T38631; T38631.
DR RefSeq; NP_594015.1; NM_001019441.2.
DR AlphaFoldDB; O14110; -.
DR SMR; O14110; -.
DR BioGRID; 279624; 1.
DR STRING; 4896.SPAC31G5.14.1; -.
DR iPTMnet; O14110; -.
DR MaxQB; O14110; -.
DR PaxDb; O14110; -.
DR PRIDE; O14110; -.
DR EnsemblFungi; SPAC31G5.14.1; SPAC31G5.14.1:pep; SPAC31G5.14.
DR GeneID; 2543195; -.
DR KEGG; spo:SPAC31G5.14; -.
DR PomBase; SPAC31G5.14; gcv1.
DR VEuPathDB; FungiDB:SPAC31G5.14; -.
DR eggNOG; KOG2770; Eukaryota.
DR HOGENOM; CLU_007884_10_0_1; -.
DR InParanoid; O14110; -.
DR OMA; MPVQYPA; -.
DR PhylomeDB; O14110; -.
DR Reactome; R-SPO-6783984; Glycine degradation.
DR PRO; PR:O14110; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005960; C:glycine cleavage complex; ISS:PomBase.
DR GO; GO:0005759; C:mitochondrial matrix; IC:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0004047; F:aminomethyltransferase activity; ISS:PomBase.
DR GO; GO:0008483; F:transaminase activity; ISS:PomBase.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; ISS:PomBase.
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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..387
FT /note="Probable aminomethyltransferase, mitochondrial"
FT /id="PRO_0000010765"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 127
FT /note="E -> G (in Ref. 1; BAA12709)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="A -> S (in Ref. 1; BAA12709)"
FT /evidence="ECO:0000305"
FT CONFLICT 257..261
FT /note="MCLYG -> NVAFME (in Ref. 1; BAA12709)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="I -> T (in Ref. 1; BAA12709)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 42408 MW; 68A3CBDCFF84C45A CRC64;
MNRSAALSIL KRQSSTAASS SLKRTPLYDL HLKEGATIVP FAGFSMPVQY KGQTISASHK
WTREHSGLFD VSHMVQWFVR GENATAYLES ITPSSLKELK PFHSTLSAFT NETGGIIDDT
IISKQDENTY YIVTNAACSE KDEANLKKHI ENWKGVELER VQGRALIAIQ GPETASVVQK
LIPNVDFSVL KFGQSAYVDF KGVKCLFSRS GYTGEDGFEV SIPEEVSVDF ASTLLADTRV
RPIGLGARDT LRLEAGMCLY GSDIDDTTSP VEGSLSWIIG KRRRKEGGFV GSSRILKELK
DGPSRRRVGF IVEKVPARHG SAVEVDGVEV GQVTSGCPSP TLGKNIAMGY ISTGLHQVGT
PAHIKVRNKL HPAQVVRMPF VETHYYK
