ID A0A1Y2X0G5_9PEZI Unreviewed; 1053 AA.
AC A0A1Y2X0G5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=K445DRAFT_75371 {ECO:0000313|EMBL:OTB15433.1};
OS Daldinia sp. EC12.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Daldinia.
OX NCBI_TaxID=1001832 {ECO:0000313|EMBL:OTB15433.1, ECO:0000313|Proteomes:UP000243732};
RN [1] {ECO:0000313|EMBL:OTB15433.1, ECO:0000313|Proteomes:UP000243732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC12 {ECO:0000313|EMBL:OTB15433.1,
RC ECO:0000313|Proteomes:UP000243732};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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; KZ112939; OTB15433.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2X0G5; -.
DR STRING; 1001832.A0A1Y2X0G5; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000243732; 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:UP000243732};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 66..516
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 548..823
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 868..989
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 796
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1053 AA; 115626 MW; A46D8E526C735E86 CRC64;
MYRLDIHRLV QLRASTSLSS RLQRTAPWIC HNCTYKAVTI ATQRRSFTAI DRTQVANYAD
LDTFPRRHIG PDEADTAEML KALSPPVDNL DKFVQQVIPA NILSKKKLEI PPHNGPQSES
SLKAKVKEYQ SNITVKKSFL GQGYYGTHTP AVIQRNVLEN PAWYTSYTPY QPEISQGRLE
SLVNFQTVVT DLTGLPIANA SLLDEGTAAA EAMTLSMNAL STSRAKREGK TFVVSKSLHP
QTISVLRARA DGFGIKILEL DVSKDEARAE IENIGEDLVG VMVQYPDTYG HVENFQPLAD
LVHKQCALLS VATDLLALTM LKPPGEWGAD IAFGSAQRFG VPLGFGGPHA AFFAVQEKHK
RKMPGRLIGL SKDRLGGKAY RLALQTREQH IRREKATSNV CTSQALLANM NALYAIYHGP
EGLKAIAERV VRGARVVQAI AEENGFGTEK SKWISNGSVL FDTVIIDVGS KENQAQSVST
AHEHGMYIRQ IGEKQIGISV DETTSLDDLV KVFQVFATAA GNTKASAYDA AEGRVRQLLE
KHADSVDIPD AFKRTSSFLT HPVFNTHHSE TELLRYIYHL QSKDLSLVHS MIPLGSCTMK
LNGTTEMSLI TLPEFSQIHP YTPQEMVPGY NSLLEMFREQ LRNITGMDAV SLQPNSGAQG
EFAGLRAIRE YHKAQGSGGK KRDICLIPVS AHGTNPASAA MAGMRVVPIK CDTTTGNLDL
ADLEAKCKKH QEELGAIMVT YPSTFGVFEP EIKKVCELVH EHGGLVYMDG ANMNAQIGLC
SPGEIGADVC HLNLHKTFCI PHGGGGPGVG PICVKQRLQP YLPRDPNAEG KATSGGYAVS
SANNGSASIN LISWAYNTLM GADGLTQATK ITLLNANYIL SRLKPHYQIL YVNEHGRCAH
EFILDARPFS KSAGIEAIDI AKRLQDYGFH APTMSWPVAN TLMIEPTESE SKEELDRFID
ALISIRGEIR EIEEGKAPRE GNVLKMSPHT MQDLIAGDGG EGGKWERSYS REKAAYPLPW
LKEKKFWPTV TRVDDTYGDL NLFCTCPPVE DTT
//
