ID A0A8H5AWV1_9AGAR Unreviewed; 1000 AA.
AC A0A8H5AWV1;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 15.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=D9619_002853 {ECO:0000313|EMBL:KAF5312390.1};
OS Psilocybe cf. subviscida.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Psilocybe.
OX NCBI_TaxID=2480587 {ECO:0000313|EMBL:KAF5312390.1, ECO:0000313|Proteomes:UP000567179};
RN [1] {ECO:0000313|EMBL:KAF5312390.1, ECO:0000313|Proteomes:UP000567179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101986 {ECO:0000313|EMBL:KAF5312390.1,
RC ECO:0000313|Proteomes:UP000567179};
RX PubMed=32382073; DOI=10.1038/s41396-020-0667-6;
RA Floudas D., Bentzer J., Ahren D., Johansson T., Persson P., Tunlid A.;
RT "Uncovering the hidden diversity of litter-decomposition mechanisms in
RT mushroom-forming fungi.";
RL ISME J. 14:2046-2059(2020).
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. {ECO:0000256|RuleBase:RU364056}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage complex H protein]
CC + glycine + H(+) = N(6)-[(R)-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 Evidence={ECO:0000256|ARBA:ARBA00049026,
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:KAF5312390.1}.
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DR EMBL; JAACJJ010000056; KAF5312390.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8H5AWV1; -.
DR OrthoDB; 6537869at2759; -.
DR Proteomes; UP000567179; Unassembled WGS sequence.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:TreeGrafter.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016594; F:glycine binding; IEA:TreeGrafter.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:TreeGrafter.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:TreeGrafter.
DR CDD; cd00613; GDC-P; 1.
DR FunFam; 3.90.1150.10:FF:000097; Glycine cleavage system P protein; 1.
DR FunFam; 3.40.640.10:FF:000005; Glycine dehydrogenase (decarboxylating), mitochondrial; 1.
DR FunFam; 3.40.640.10:FF:000007; glycine dehydrogenase (Decarboxylating), mitochondrial; 1.
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 NCBIfam; NF003346; PRK04366.1; 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|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR603437-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000567179};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 49..481
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 493..772
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 821..941
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 748
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1000 AA; 108473 MW; D9D3FB5F7D7B44F6 CRC64;
MALIHCRPAL GRLAASSRLN RVFFFNVRRG LASLKPLPSL FAPLDTFAER HIGPDDAEAS
KMLNQLGYES MDAFVAETVP PKIRVSAHSV DNTSIPVYSE SQLHARAKQL AGQNKPFKSY
IGMGYHCAVV PPVILRNVME NPAWYTPYTP YQPEIAQGRL ESLINFQTMV TSLTSMDIAN
ASLLDEATAA AEGMVMAHVS APKKKTFIVD TGVVPQTLSV LRTRAKGFGI NIVVGDAGKL
LQDEATRSHV CGVLVQYPDV DGNIKDFGAL ASTVHSLGAL IVCATDLLAL TKIKPPGEWG
ADIVVGNSAR FGVPAGYGGP HAAFFAVTDK LKRKMPGRLV GRSRDAEGKP AYRLSLQTRE
QHIRREKATS NICTSQALLA NMAAMYAVYH GADGLQRIAT KVHKFTQVLQ TAVESMGYKT
VNKNFFDTLT LDVSAIGTAD FVHNTAIAAG INFRRIDEKH IGVTLDESVS PDDFLALLNI
FSTAASARPL TLSELSDPKS PSIPTELQRT SEYLPHPVFN KHHSETEMLR YINHLASKDL
SLVHSMIPLG SCTMKLNSTS SMIPLTWPEF SAVHPFAPYD QVKGYHQVIG ELESDLCKIT
GFAAASLQPN SGAAGEYAGL CVIRAYHESR GDSHRDICLI PLSAHGTNPA SAAMAGLKVV
AVKVHPDGNL DLEDLRTKAE KHKDHLAAFM ITYPSTFGVF ESGVQDACKI IHDNGGQVYL
DGANLNAQIG LTNPATCGGD VCHMNLHKTF AIPHGGGGPG VGPICVAAHL APFLPKHPAM
PSFNSQAIDA VSAAPFGSAS INLISWAYIK MLGGAGLVES SKIALLNANY MASRLQGHYS
LKYKNENGRV AHELLIDLAE FGKAAGLKVT DFAKRLQDFG FHPPTCSWPI QTCMLIEPTE
SETLEELDRF CDAMIQIRNE AEDIITGKQP KDNNVLKNAP HTVSVIGSSE WNRPYTREQA
AYPLSWLREK KFWPSVSRID DAYGDLNLIC DCPSVEEMAQ
//
