ID F0ZJ64_DICPU Unreviewed; 1006 AA.
AC F0ZJ64;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=DICPUDRAFT_78309 {ECO:0000313|EMBL:EGC36024.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC36024.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. {ECO:0000256|RuleBase:RU364056}.
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 Evidence={ECO:0000256|ARBA:ARBA00043839,
CC ECO:0000256|RuleBase:RU364056};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR603437-50, ECO:0000256|RuleBase:RU364056};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|RuleBase:RU364056}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|RuleBase:RU364056}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000256|ARBA:ARBA00010756,
CC ECO:0000256|RuleBase:RU364056}.
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DR EMBL; GL871040; EGC36024.1; -; Genomic_DNA.
DR RefSeq; XP_003287462.1; XM_003287414.1.
DR AlphaFoldDB; F0ZJ64; -.
DR STRING; 5786.F0ZJ64; -.
DR EnsemblProtists; EGC36024; EGC36024; DICPUDRAFT_78309.
DR GeneID; 10500347; -.
DR KEGG; dpp:DICPUDRAFT_78309; -.
DR eggNOG; KOG2040; Eukaryota.
DR InParanoid; F0ZJ64; -.
DR OMA; RNLICTC; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR HAMAP; MF_00711; GcvP; 1.
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 {ECO:0000256|RuleBase:RU364056};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364056};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50,
KW ECO:0000256|RuleBase:RU364056};
KW Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 47..481
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 507..785
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 827..948
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 754
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1006 AA; 110799 MW; 75F158DC5B9964CF CRC64;
MFRLLARNAL KQTSILNAST KNVVLIRNNT STTQKVSVFQ PLDTFPKRHI GPNENEISEM
LKQISTSKLS NKTPSSLDQL IEYTIPKDIR LNKVLDIEGN PIIGESQLLK ELKQVAQKNK
IFRSFIGMGY YNTLTPHVIQ RNILENPGWY TPYTPYQAEI SQGRLESLLN FQTMVSELTA
LPMANASLLD EATAAAEAVT MCINISKSKG PFTFLVDSNC HPQTIDTIKT RAEPKGIRIE
ISEPKDFDFS LAGVVGCIVQ YPATNGSVAD IKELADRAHQ ANSLVVAATD LLSLAMIKAP
GEWGADIALG NSQRFGVPLG FGGPHAAFFA TKDKYARLLP GRIIGVSKDK QGDPAYRMAL
QTREQHIRRE KATSNICTSQ ALLANMSAMY AVYHGQEGIK AIANTVHRKT IILREGISRM
GYQVLDRPFF DTILIESGDK TEMIIKDLAA KKINVRKYDN KSIAISIDET VTAEDITNLL
DGFVAHASKP LGLASPQQLE ADTNSTKVIP AELERTSEFL THPIFNKYHS EHELLRYIHK
LQKKDLGLTT AMIPLGSCTM KLNATTEMYP VSWPEFNSLH PFVPSDQTLG YKEMFNSISK
SLCEITGFDG CSLQPNAGSQ GEYAGLMVIR SYLISIGQSQ RNVCLIPVSA HGTNPASAAM
VGMKVVVVDC DAQGNIDQND LRAKAEKYKD TLAALMITYP STHGVFEEGA KDMCDIVHRY
GGQVYMDGAN MNAQVGLCRP GDIGADVCHL NLHKTFCIPH GGGGPGMGPI CVKSHLSPFL
PGHSVVQNAG GERAMSAVSA APWGSSSILP ITYVYLKLMG GQGLKKATQV AILSANYMAS
RLKDHYKILY TGSHGLVAHE FIIDLRMFKE SAGIEAEDVA KRLQDMNFHG PTMSWPVPNT
LMIEPTESES KYELDRLCDA LIIIREEIRE IEEGRADKKN NVLVNSPHTE KVIINEKWNY
PYTREKAAFP TPATKLSKFW PTVGRIDNVH GDKNLVCSCP PLSDYQ
//
