ID A0A166YQH8_9PEZI Unreviewed; 1058 AA.
AC A0A166YQH8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=CT0861_11939 {ECO:0000313|EMBL:KZL77939.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL77939.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL77939.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL77939.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-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:KZL77939.1}.
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DR EMBL; LFIV01000004; KZL77939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166YQH8; -.
DR STRING; 708197.A0A166YQH8; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000076552; 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 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:UP000076552};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 85..531
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 556..835
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 873..994
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 806
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1058 AA; 114512 MW; 1D5B4BCA80DC5DF5 CRC64;
MASLRLPLPR QLRLAAPRSR VLARQTPASS WVCNSCASNS TVISRVPRVR TFSAITSLQN
ATSARIASVD ASLEPLQRPE SFIPRHIGPD VHDVEAMLKA LDPPAKSIDE FIAQVLPADV
ISERKSFAWD TEGPTDESKI LARATAWAKA NEAAPKPLIG AGYSPSVTPR VIQTNVLESP
AWYTSYTPYQ PEISQGRLES LLNYQTMVSD LTGLPISNAS LLDEGTAAAE AMTLSMNALS
ASRAKRPGKT FVVSHLVHPQ SISVLRSRAQ GFGIKVEVLD VSTAETQEKI KTLGQDLVGV
MVQYPDTRGK VEDFKGLSEL VHSQGALLSA ATDLLALTVL TPPGEWGADI AFGSAQRFGV
PLGFGGPHAA FFAVKEAHKR RMPGRLVGVS KDRTGRRALR LALQTREQHI RREKATSNVC
TAQALLANMA ALFAVYHGPE GLKEIASRLV RLARGVQAVA EAAGLKTEQS GASPDGKVLF
DTVVIKASDR SQNILAEAKK AGLGFRDYGN GDIGISVNEN VNEEVFNTIA AVLGSATGTQ
TAEIASKAYG ALTQDITELL PESLRRQSAY LTHPVFNTHR SETEILRYIH HLQSKDLSLV
HSMIPLGSCT MKLNSATEMA LISLPGFSTI HPHTPPSELK GYTALIESLS EQLKGITAMD
AVSLQPNSGA QGEFAGLRVI RKYLEQQPGK KRDICLIPVS AHGTNPASAA MAGMRVVPIK
CDQKTGNLDI EDLEAKCKKH ADELGAFMVT YPSTYGVFEP SVKKACDLVH QYGGQVYMDG
ANMNAQIGIC SPGEIGADVC HLNLHKTFCI PHGGGGPGVG PICVKEHLGP YLPGRTPEAE
EAMVASAPYG SAGILPISWA YNALMGNDGL RLATKTAILN ANYILARLKP HYKILYTNEN
GRCAHEFILD ARPFSATAGV EAIDIAKRLQ DYGFHAPTMS WPVANTLMIE PTESESKEEL
DRFVDTLISI REEIREVEEG KQPREGNVLK MAPHPQMDVI LGDGEGKWDR PYTREKAAYP
LPHLKEKKFW PSVARVDDTY GDLNLFCTCP PVEDTTQE
//
