ID A0A9P7W544_9AGAR Unreviewed; 996 AA.
AC A0A9P7W544;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=BT62DRAFT_926528 {ECO:0000313|EMBL:KAG7452322.1};
OS Guyanagaster necrorhizus.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Guyanagaster.
OX NCBI_TaxID=856835 {ECO:0000313|EMBL:KAG7452322.1, ECO:0000313|Proteomes:UP000812287};
RN [1] {ECO:0000313|EMBL:KAG7452322.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MCA 3950 {ECO:0000313|EMBL:KAG7452322.1};
RG DOE Joint Genome Institute;
RA Koch R.A., Yoon G., Arayal U., Lail K., Amirebrahimi M., Labutti K.,
RA Lipzen A., Riley R., Barry K., Henrissat B., Grigoriev I.V., Herr J.R.,
RA Aime M.C.;
RT "Adaptations for nitrogen fixation in a non-lichenized fungal sporocarp
RT promotes dispersal by wood-feeding termites.";
RL Submitted (NOV-2020) 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=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:KAG7452322.1}.
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DR EMBL; MU250524; KAG7452322.1; -; Genomic_DNA.
DR RefSeq; XP_043045822.1; XM_043185058.1.
DR AlphaFoldDB; A0A9P7W544; -.
DR GeneID; 66107355; -.
DR OrthoDB; 6537869at2759; -.
DR Proteomes; UP000812287; 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 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|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR603437-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000812287};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 46..479
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 512..771
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 743
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 996 AA; 108177 MW; E959967C0B8C5C1D CRC64;
MAFARCALGF HRPALAVPCC RSVHGVRNLA TARQFDLLAP LDTFQERHIG PNEHQVSQML
SRVGYDSMDA FIADTVPPKI RVSTADISNR TIPSFSESEL HARAKALAGQ NVAFKSYIGM
GYHSAVVPPV ILRNVMENPQ WYTPYTPYQP EIAQGRLESL VNYQTMIMSL TSMDIANASL
LDEATAAAEG MVMAFVSSGH KKRTFLVDSG VLPQTISVLR TRAKGFGIKV LVEDATVAIK
HQSLQSDLCG VLVQYPDVDG NIKDFGGLAV TAHSSDALVA CATDLLALTM LKPPGEWGAD
IVFGNSARFG VPSGYGGPHA AFFAVTDKLK RKMPGRLIGR SRDAAGRPAY RLALQTREQH
IRRERATSNV CTSQALLANM AAMYAVYHGP VGLQRIANKV HVTAQIFKSS VESLGYKLSN
STFFDTITLD VSVAGGAQTV HDIAKSARVN LRSIDDHHVG VTFDESVTQA DLEALVAIFA
SAVKSSGQLI LPSEGSPIPS YLQRTSDYLR HPVFNKHHSE TEMLRYMNHL VSKDLGLVHS
MIPLGSCTMK LNSTSSMIPL TWPEFSAVHP FAPHDQVEGY LSIIKELEDD LCKITGFHAA
SLQPNSGAAG EYAGLCVIRT YHESRGEGHR DICLIPLSAH GTNPASAVMA GLKVVPVKAL
SDGSLDLEDL TAKAEKHKDN LAAFMITYPS TFGVFEDGVQ DACKIIHDNG GQVYLDGANL
NAQIGLTNPA TCGGDVCHMN LHKTFAIPHG GGGPGVGPIC VAEHLSPFLP SHRSLPQTAD
SRAIEAVSAA PFGSASIHLI SWAYIKMLGG RGLVDSSKVA LLNANYMASR LSEHYNVRYT
NKHGRVAHEL LIDLAEFDKS AGLKVTDFAK RLQDYGFHPP TCSWPTSTCM LIEPTESEPL
EEIDRFCDAM IQIRREAEDV VTGNQPRDNN VLKNAPHPVS VLAEEEWSRP YSRRTAVYPL
AWLSEKKFWP TASRIDDAYG DLNLICDCPS VQEVAS
//
