ID   GCSP_DICDI              Reviewed;         994 AA.
AC   Q54KM7;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=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=gcvP; ORFNames=DDB_G0287255;
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. 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 (By similarity). {ECO:0000250}.
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   -!- SUBUNIT: Homodimer. The glycine cleavage system is composed of four
CC       proteins: P, T, L and H. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000305}.
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DR   EMBL; AAFI02000099; EAL63829.1; -; Genomic_DNA.
DR   RefSeq; XP_637330.1; XM_632238.1.
DR   AlphaFoldDB; Q54KM7; -.
DR   SMR; Q54KM7; -.
DR   STRING; 44689.DDB0231130; -.
DR   PaxDb; Q54KM7; -.
DR   EnsemblProtists; EAL63829; EAL63829; DDB_G0287255.
DR   GeneID; 8626028; -.
DR   KEGG; ddi:DDB_G0287255; -.
DR   dictyBase; DDB_G0287255; gcvP.
DR   eggNOG; KOG2040; Eukaryota.
DR   HOGENOM; CLU_004620_3_2_1; -.
DR   InParanoid; Q54KM7; -.
DR   OMA; CVPMSEY; -.
DR   PhylomeDB; Q54KM7; -.
DR   Reactome; R-DDI-6783984; Glycine degradation.
DR   PRO; PR:Q54KM7; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; 3.40.640.10; -; 2.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
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..21
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..994
FT                   /note="Glycine dehydrogenase (decarboxylating),
FT                   mitochondrial"
FT                   /id="PRO_0000327611"
FT   MOD_RES         742
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   994 AA;  109578 MW;  920A98C4A51F90D0 CRC64;
     MLKLLRNNGI NKLKSNLIRN YSTKQSIFQA LDTFPKRHIG PNENEINEML KSINTSKLSK
     KNPNSLEQLI EYTIPKDIRL NRELNIEENK VIGENQLLKD LKKIAEKNKV YRSFIGMGYY
     GTITPHVIQR NILENPGWYT PYTPYQAEIS QGRLESLLNF QTMVSEFTGL PMSNASLLDE
     ATAAAEAMQM CVNISKSKGP FAFLVDKYCH PQTIDTIKTR AEPKGIRIEV VDSKDFKFTE
     DVVGCIVQYP SSNGVITDYK EMADRAHQAN ALVVAATDLL SLALLKPPGE WGADIALGNS
     QRFGVPLGFG GPHAAFFSTK DKYARLLPGR IIGVSKDKQG NSAFRMALQT REQHIRREKA
     TSNICTSQAL LANMSAMYAV YHGQQGIKDI ANAVHRKAII LAEGIKRLGY TVLDRPFFDT
     VLIITGDKTD MMIKELESRQ INVRQYCSKS ISISLDETVT SADISALLNG FSAHASKPLG
     LSSPEQLEKE TSTISVISEE FARQTPFLTH PIFNRYHSEH ELLRYIHKLQ KKDLGLTTAM
     IPLGSCTMKL NATTEMYPVS WPEFNSIHPF VPANQSLGYK EMFESISNML CEVTGFDGCS
     LQPNAGSQGE YAGLMVIRSY LTSIGQSQRN VCLIPVSAHG TNPASAAMVG MKVVVVDCDT
     NGNIDVADLK AKAEKHKDTL AALMITYPST HGVFEEGAND ICDIIHANGG QVYMDGANMN
     AQVGLCRPGD IGADVCHLNL HKTFCIPHGG GGPGMGPICV KSHLAPFLPG HSVVKGVGGE
     RAMSAVSAGP WGSSSILPIT YVYLKLMGGQ GLKKATQVAI LNANYMASRL KDHYKILYTG
     SHGLVAHEFI IDLRMFKESA GIEAEDVAKR LQDMNFHGPT MSWPVPNTLM IEPTESESKY
     ELDRLCDALI LIREEIREIE TGKADRKNNV LVNSPHTEKV IVADNWNYPY SRSKAAFPTP
     ATVASKFWPT VGRIDNVHGD KNLVCSCPPL SDYQ