ID A0A0W8DC15_PHYNI Unreviewed; 998 AA.
AC A0A0W8DC15;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=AM587_10003314 {ECO:0000313|EMBL:KUF93869.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF93869.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUF93869.1, ECO:0000313|Proteomes:UP000052943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUF93869.1}.
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DR EMBL; LNFO01001208; KUF93869.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W8DC15; -.
DR STRING; 4790.A0A0W8DC15; -.
DR EnsemblProtists; KUF93869; KUF93869; AM587_10003314.
DR OMA; RNLICTC; -.
DR Proteomes; UP000052943; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
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:UP000052943};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 36..467
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 476..770
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 817..937
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 739
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 998 AA; 108183 MW; 97FA165C95E6CCFD CRC64;
MLLQRVLSVR RVTLARAVAA RAMATSSYAP ADAFLHRHLG VSSEKDRKAM LATVGFDSVE
DLVAAAVPTE IRLDKPLDLP PPLSESEALA KLKVLAAKNQ TLKSFIGMGF NDTHTPAPIV
RHILENPGWY TSYTPYQAEV SQGRLEMLLN FQTMILDLTG LEYANASLLD EATAAAEAMA
LAHGNFNGKR TKFFVDQDAH PQTIGMMQTR ADNFGIELVV GNPKTDLDLK DQGYSGVLLQ
YPTTFGAVND YRDFVDEAHK SKLVVAVATD PLSLTQLTPP GEWGADIALG SAQRFGVPMM
FGGPHAAFLA TTKKYHRKMP GRIIGVSVDS RGEPAVRMAM QTREQHIRRD KATSNICTAQ
ALLANMAAAY AIYHGPDGLD IIAKRANLYA ATLAAGLEKF APKCKVVNDA FFDTLEIDVS
QSGTSAADVA AEATKRGVNV RVIDDKRVGV SMGESVDLKD LEKLLLAFGA EESLPKDLAE
ALGARAEEIQ KKSIPEGLRR STSYLDHDIF HKYRSETELT RYLKQLEDKD LALNRSMISL
GSCTMKLNAV SELAPISWPE FTNVHPFVPE EQSAGYRELI ESLNHSLAVI TGFSAVSTQP
QSGAQGEYAG LLTIRNYQRS IGQGHRNVCL IPVSAHGTNP ASAVMAGMKV VVVKSDENGH
VDREDLAAKA AEHSDNLSAF MITYPSTFGM FEPGIKDMVD LIHSHGAQVY MDGANMNAQV
ALCNPGGIGA DVCHLNLHKT FCIPHGGGGP GVGSIGVAAH LAPFLPGHTV MPTGGEGEHT
VKKTDSAVSG SPFGSAGILP IPWMYINMLG EDGLKQATST AILNANYMAK KLESHYEVVF
RSANGTCAHE FIIDMRPFKE LGIVEEDVAK RLQDFGFHSP TMSWPVPGTL MIEPTESESK
AEMDRFCEAL AIIRREIEDV ATGAIAVEDS PLKHAPHTVD QVTAGVWDRK YSREQAAFPA
PWHQGGKNKT YWPSVGRVDN VHGDRHLVCS CPPLSDYE
//
