ID A0A2J6Q0K6_9HELO Unreviewed; 1054 AA.
AC A0A2J6Q0K6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=NA56DRAFT_646747 {ECO:0000313|EMBL:PMD19820.1};
OS Hyaloscypha hepaticicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD19820.1, ECO:0000313|Proteomes:UP000235672};
RN [1] {ECO:0000313|EMBL:PMD19820.1, ECO:0000313|Proteomes:UP000235672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD19820.1,
RC ECO:0000313|Proteomes:UP000235672};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (MAY-2016) 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}.
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DR EMBL; KZ613487; PMD19820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6Q0K6; -.
DR STRING; 1745343.A0A2J6Q0K6; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000235672; 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:UP000235672};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 84..537
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 584..839
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 882..1003
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 810
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1054 AA; 114810 MW; 101D2789422D94F8 CRC64;
MAASSLALRT QLGRLASRSG SSIRRTPSQL TRSRICRHCS QSGFSSASIG RRTFYTSSAS
DEANSLPTAA ASRGAYLPLD TFARRHIGPS TDSTEQMLKA LDPPVKNLDD FIKQVLPSDI
LSSTDLEIDA ARSGGEEGFT ESQLLARLRA IASKNTIMRS YIGCGYAGTR VPEVIKRNVL
EGPGWYTSYT PYQPEISQGR LESLLNFQTL VCDLTALPIS NASLLDESTA AAEAMTLSMN
ALPASRLKGK SKTFLVSHLV HPQTKAVLQS RADGFDIKIE VADVLADGGK RIKELDKDLV
GVLVQYPDTE GGVEDFKGLA NTIHDQGATF SVATDLLALT VLTPPGEFGA DIAFGNAQRF
GVPFGYGGPH AAFFAVSEKY KRKIPGRLIG VSKDRLGDKA MRLALQTREQ HIRREKATSN
VCTAQALLAN MSAFYAIYHG PQGLRNIAER AINGARILEQ GLKNLGFETG SRGKGEDGRV
LFDTVVVNVG QGKSDEVMQH AMKAYYINLR KFDDSRLGIT VDETVDTKDL EEILSIFKVF
ASSKEDAHID QIIESLPNGG KLELPASFKR TSEYLTHPVF NSHHSETELL RYIHHLQSKD
LSLTHSMIPL GSCTMKLNAT TEMAPVTWPE FSSLHPFAPT DQAAGYKIMI DELEADLAKI
TGFDAVSLQP NSGAQGEFTG LRVIRKYQEQ QPGKKRDICL IPVSAHGTNP ASAAMAGMRV
VTVKCDTKSG NLDMADLKSK CEKYSEELGA IMITYPSTFG VFEPEIKAVC DVVHQHGGQV
YMDGANMNAQ IGLCSPGEIG ADVCHLNLHK TFCIPHGGGG PGVGPIGVKS HLAPFLPGHP
LVKTGGEKAI APVSGAPWGS ASILPISWAY IKMMGGRGLT HATKITLLNA NYIMSRLRPH
YPILYTNANA RCAHEFILDV RGFKESAGIE AIDVAKRLQD YGFHAPTMSW PVANTLMIEP
TESESKEELD RFINALISIR EEIKAVEDGK APREGNVLKM APHTQKDLIV GEWDRPYTRE
QAAYPLPWLK EKKFWPSVTR LDDGTKTSLE LPLP
//
