ID GCSP_SCHPO Reviewed; 1031 AA.
AC Q09785;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 27-MAR-2024, entry version 150.
DE RecName: Full=Putative glycine dehydrogenase (decarboxylating), mitochondrial;
DE EC=1.4.4.2;
DE AltName: Full=Glycine cleavage system P protein;
DE AltName: Full=Glycine decarboxylase;
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring);
DE Flags: Precursor;
GN Name=gcv2; ORFNames=SPAC13G6.06c;
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 [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).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. The P protein binds the alpha-amino group of glycine through
CC its pyridoxal phosphate cofactor; CO(2) is released and the remaining
CC methylamine moiety is then transferred to the lipoamide cofactor of the
CC H protein.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC L-lysyl-[glycine-cleavage complex H protein]; Xref=Rhea:RHEA:24304,
CC Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10495, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57305, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83143; EC=1.4.4.2;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAA91099.2; -; Genomic_DNA.
DR PIR; S62435; S62435.
DR RefSeq; NP_592832.2; NM_001018233.2.
DR AlphaFoldDB; Q09785; -.
DR SMR; Q09785; -.
DR BioGRID; 279275; 1.
DR STRING; 284812.Q09785; -.
DR MaxQB; Q09785; -.
DR PaxDb; 4896-SPAC13G6-06c-1; -.
DR EnsemblFungi; SPAC13G6.06c.1; SPAC13G6.06c.1:pep; SPAC13G6.06c.
DR GeneID; 2542828; -.
DR KEGG; spo:SPAC13G6.06c; -.
DR PomBase; SPAC13G6.06c; gcv2.
DR VEuPathDB; FungiDB:SPAC13G6.06c; -.
DR eggNOG; KOG2040; Eukaryota.
DR HOGENOM; CLU_004620_3_2_1; -.
DR InParanoid; Q09785; -.
DR OMA; RNLICTC; -.
DR Reactome; R-SPO-6783984; Glycine degradation.
DR PRO; PR:Q09785; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IC:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0016594; F:glycine binding; IBA:GO_Central.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
DR CDD; cd00613; GDC-P; 2.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR InterPro; IPR003437; GcvP.
DR InterPro; IPR049316; GDC-P_C.
DR InterPro; IPR049315; GDC-P_N.
DR InterPro; IPR020581; GDC_P.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00461; gcvP; 1.
DR PANTHER; PTHR11773:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR Pfam; PF21478; GcvP2_C; 1.
DR Pfam; PF02347; GDC-P; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE 3: Inferred from homology;
KW Mitochondrion; Oxidoreductase; Pyridoxal phosphate; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..49
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 50..1031
FT /note="Putative glycine dehydrogenase (decarboxylating),
FT mitochondrial"
FT /id="PRO_0000010751"
FT MOD_RES 783
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1031 AA; 114233 MW; 1AAB78E5A0D88F7B CRC64;
MFDSFMKRNQ LALIMFRACS KLQYHGVNTS LSRHLFLAKR NLSISSACLE AKNSQKFPAL
DTFEPRHIGP SKTDQQYQLE SLGYKDFDSF LKDVIPDSVR TPESQLMAFG SVNPNEKNPP
VNYSESEFTT LANNVANQNK LIKSFIGMGY YNVKLPAAIQ RNVLENPEWY TQYTPYQAEI
SQGRLESMMN YQTMIADLTG LSISNASLLD EGTAAGEAMV MLMANDKKKR KTFLVDKNIY
PNTLSVLRTR ASGFGIKIEL DNITPELITK SAKHVFGIFV QYPAADGSIF DYGHLAATAR
SFNMHVVAAT DLLALTILKS PGEWGADVAV GSTQRFGLPM GYGGPHAGFF ACSEEFKRKI
PGRLIGLSKD RLENPAYRLA LQTREQHIRR EKATSNICTA QALLANMSAF YAIYHGPNGL
QEIANRIYAS TSFLKSALES SGYKIVNKSH FFDTLTIEVE SADKVLAKAL DHGYNLRKVD
DSHVGLSLDE TVCDKDIQAL FSIFNINKSV DQYYMEIATS EPNGNSASTV DNLSICSLPE
NFRRTTLYLQ HPVFNRYHSE TELMRYIHHL QSKDLSLAHA MTPLGSCTMK LNAVTEMMPI
TNPLFANIHP YVPEEQAKGY RHVIEDLQLM LTTITGFDAA CFQPNSGAAG EYTGLSVIRA
YQRSIGQGHR NICLIPVSAH GTNPASAAMA GFTVIPVKCL NNGYLDMQDL KEKASKHADK
LAAFMVTYPS TFGIFEPDVK EALEVIHEHG GQVYFDGANM NAMVGLCKAG DIGADVCHLN
LHKTFCIPHG GGGPGVGPIC VKKHLADFLP SHPVVSCGGK NGITSVSSSP FGSAGILPIS
WAYMRMMGLA GLRDASKAAL LNANYMAKRL SSHYKLVYTN KNNLCAHEFI LDAREFKATA
GVDATDIAKR LQDYSFHAPT LSWPIANTLM IEPTESESMY EMDRFCDALI SIRQEIREIE
EGLQPKDNNL LVNAPHPQKD IASEKWDRPY TRERAVYPVP LLKERKFWPS VARLDDAYGD
KNLFCTCSPV V
//
