ID A0A2A9NN53_9AGAR Unreviewed; 996 AA.
AC A0A2A9NN53;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=AMATHDRAFT_76072 {ECO:0000313|EMBL:PFH49697.1};
OS Amanita thiersii Skay4041.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pluteineae; Amanitaceae; Amanita.
OX NCBI_TaxID=703135 {ECO:0000313|EMBL:PFH49697.1, ECO:0000313|Proteomes:UP000242287};
RN [1] {ECO:0000313|EMBL:PFH49697.1, ECO:0000313|Proteomes:UP000242287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKay4041 {ECO:0000313|EMBL:PFH49697.1,
RC ECO:0000313|Proteomes:UP000242287};
RG DOE Joint Genome Institute;
RA Hess J., Skrede I., Wolfe B., LaButti K., Ohm R.A., Grigoriev I.V.,
RA Pringle A.;
RT "Transposable element dynamics among asymbiotic and ectomycorrhizal Amanita
RT fungi.";
RL Submitted (FEB-2014) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KZ302022; PFH49697.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9NN53; -.
DR STRING; 703135.A0A2A9NN53; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000242287; 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; 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|PIRSR:PIRSR603437-50,
KW ECO:0000256|RuleBase:RU364056};
KW Reference proteome {ECO:0000313|Proteomes:UP000242287};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 41..475
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 487..771
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 814..935
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 742
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 996 AA; 108182 MW; 3873DA577BE060E7 CRC64;
MVSLRYVQPL TRLSRLLPLS RPFASLKKPS SLFSPLDSFQ ERHVGPDDAE TSKMLSRLGY
SSMDAFINET VPHKIRLPPS SLDNSSIPVL SESQLHERAK SLGASNKTYK SYIGMGYHCA
VVPPVILRNV MENPAWYTPY TPYQPEIAQG RLESLLNFQT MVTSLSSMDV ANASLLDEAT
AAAEAMVMAF VSASNKKPTF IVDSGVLPQT LAVLRTRAKG FGISIVVGDA AGLVNDKTIM
SNCCGVLVQY PDVDGNVKDF DTLAKTIHAS GGLVACATDL LALTMLKPPG EWGADIVLGN
SGRFGVPAGY GGPQAAFFAV KDRLKRKMPG RLIGRSRDAN GNLAYRLSLQ TREQHIRREK
ATSNICTSQA LLANMAAMYA VYHGPDGLRR IASKVHGFTQ VFMHLVQQFG YNVENKHFFD
TVTLNVTPVV ANAGVIHEAS IAAGINLRRI DDKHVGVTLD ESVTPEDLLH LINVFASAAS
RPSILLSDLK AVDIPAIPDG LRRTSELLPH PVFNKHHSET EMLRYIFHLA SKDVGLVHSM
IPLGSCTMKL NSTSSMIPLT WPQFSAIHPF APHDQVEGYR TIIKELESDL CKITGFHAAS
LQPNSGAAGE YAGLCVIRAY HASRGEADRD ICLIPLSAHG TNPASAVMAG LKVVPVKVHT
DGTLDLEDLK AKAEKHKDKL AAFMITYPST FGVFESGVQD ACKIIHDNGG QVYLDGANLN
AQIGLTNPAT CGGDVCHMNL HKTFAIPHGG GGPGVGPICV AEHLAPFLPG HPLLESDNDK
AIDAVSAAPF GSASIHLISW AYIRMLGGHG LSEASKVALL NANYMAARLS GHYSLRFKNE
NDRVAHELLI DLAEFDKAAG LKVNDFAKRL QDYGFHPPTC SWPISTCMLI EPTESETLDE
IDRFCDAMIQ IRKEAQDIID GKQPRDNNVM KNAPHTAATL TVSDTEWNRP YSRQTAAYPL
SWLLEKKIWP SVARVDDAYG DLNLICDCPT VEELSS
//
