ID A0A2S7PUA6_9HELO Unreviewed; 1064 AA.
AC A0A2S7PUA6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=CJF30_00010383 {ECO:0000313|EMBL:PQE17878.1};
OS Rutstroemia sp. NJR-2017a BBW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Rutstroemiaceae; Rutstroemia.
OX NCBI_TaxID=2070414 {ECO:0000313|EMBL:PQE17878.1, ECO:0000313|Proteomes:UP000238072};
RN [1] {ECO:0000313|EMBL:PQE17878.1, ECO:0000313|Proteomes:UP000238072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJR-2017a BBW {ECO:0000313|EMBL:PQE17878.1,
RC ECO:0000313|Proteomes:UP000238072};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) 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:PQE17878.1}.
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DR EMBL; NJPT01000040; PQE17878.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7PUA6; -.
DR STRING; 2070414.A0A2S7PUA6; -.
DR Proteomes; UP000238072; 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:UP000238072};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 83..528
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 547..827
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 870..991
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 798
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1064 AA; 115549 MW; 09F3EB856E0ED28E CRC64;
MVASNLALRA RFAQVAIQSR STTIQRSNFT RPRVCNPCSR SVASFNSIGR RTFYNSSARD
ETNSEPSSSV SKGGYAPLDT FARRHIGPSP ECTEQMLKAL DPPVKSLDEF VKQVLPSDIL
SSKDLHVETT AEEGQEGFTE SQLLARLKSI ASENKIMRSY IGCGYAGTRV PEVIKRNVLE
GPGWYTSYTP YQPEISQGRL ESLLNYQTLV SDLTALPISN ASLLDESTAA AEAMTLSMNA
LPMARQKGKN KTFFTIAVLQ SRADGFDIKI EVGDVLADGG KRLKELGNDL IGALVQYPDT
EGGVEDFRGL GEIIHAQGAT FSVATDLLAL TVLTPPGEFG ADIAFGNAQR FGVPFGYGGP
HAAFFAVSEK YKRKIPGRLI GVSKDRLGDK AMRLALQTRE QHIRREKATS NVCTAQALLA
NMSAFYAVYH GPQGLKAIAE RAIKGARIIE AGVQKFGFET GSRGTGSDGK VLFDTVVVNV
GQGKSDEVLA HATKAYGINL RKFDDSRLGI TIDETVDTKD LHDILSLFKD FSNTDVKVEV
KELIESLGGV GIPEPLKRSS EYLTHPVFNS HHSETELLRY IHHLQSKDLS LTHSMIPLGS
CTMKLNATTE MAPVTWPEFA SIHPFVPADQ ATGYKTMIDE LEADLATITG FDAVSLQPNS
GAQGEFTGLR VIRKFQEQQP GKKRDICLIP VSAHGTNPAS AAMAGMRVVT VKCDIKSGNL
DMADLKAKCE KYSEELGAIM ITYPSTFGVF EPEIKAACDI VHQHGGQVYM DGANMNAQIG
LCSPGEIGAD VCHLNLHKTF CIPHGGGGPG VGPIGVKSHL APFLPGHPLV KTGGEKGIAP
VSGAPWGSAS ILPISWAYVK MMGGRGLTHA TKITLLNANY IMSRLRPHYS ILYTNANSRC
AHEFILDVRG FKETAGIEAI DIAKRLQDYG FHAPTMSWPV ANTLMIEPTE SESKEELDRF
INALISIRKE IQSVEDGKVP KTGNVLKNAP HSQKDLLIGE WDRPYTREQA AYPLPWLKEK
KFWPSVTRLD DAYGDLNLFC TCGPVEPVDD AENGITGAAA PQPT
//
