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   03-AUG-2022, entry version 144.
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=(R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] +
CC         glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-
CC         [glycine-cleavage complex H protein] + CO2; 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}.
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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; 4896.SPAC13G6.06c.1; -.
DR   MaxQB; Q09785; -.
DR   PaxDb; Q09785; -.
DR   PRIDE; Q09785; -.
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; CVPMSEY; -.
DR   Reactome; R-SPO-6783984; Glycine degradation.
DR   PRO; PR:Q09785; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005960; C:glycine cleavage complex; ISO:PomBase.
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; ISO:PomBase.
DR   CDD; cd00613; GDC-P; 2.
DR   Gene3D; 3.40.640.10; -; 2.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR003437; GcvP.
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   PANTHER; PTHR11773; PTHR11773; 1.
DR   Pfam; PF02347; GDC-P; 2.
DR   SUPFAM; SSF53383; SSF53383; 2.
DR   TIGRFAMs; TIGR00461; gcvP; 1.
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