ID A0A2P7YWL5_9ASCO Unreviewed; 1023 AA.
AC A0A2P7YWL5;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, 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=C7M61_000001 {ECO:0000313|EMBL:PSK40366.1};
OS [Candida] pseudohaemulonii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=418784 {ECO:0000313|EMBL:PSK40366.1, ECO:0000313|Proteomes:UP000241107};
RN [1] {ECO:0000313|EMBL:PSK40366.1, ECO:0000313|Proteomes:UP000241107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B12108 {ECO:0000313|EMBL:PSK40366.1,
RC ECO:0000313|Proteomes:UP000241107};
RA Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA Cuomo C.A.;
RT "Candida pseudohaemulonii genome assembly and annotation.";
RL Submitted (MAR-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:PSK40366.1}.
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DR EMBL; PYFQ01000001; PSK40366.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7YWL5; -.
DR STRING; 418784.A0A2P7YWL5; -.
DR EnsemblFungi; C7M61_000001_t1; PSK40366.1; C7M61_000001.
DR VEuPathDB; FungiDB:C7M61_000001; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000241107; 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:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:EnsemblFungi.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:EnsemblFungi.
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:UP000241107};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 65..499
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 528..786
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 833..958
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 759
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1023 AA; 111880 MW; 95916C3CE881ED19 CRC64;
MFRARAVVRA ARPLQLRLRA APRAPVAAFI SRSLATANTL SANYQQVHNP AKEGPTYGEL
DTFARRHFGP TPDNVAHMLK SLGYKDMDEF LTALIPPHVL VKRPLKVLPQ EGYTEQQMLK
HLHELAGKNR IAKSFIGKGY HGTIVPPVIQ RNLLELPEWY TSYTPYQPEI SQGRLESLLN
YQTMVSSLTG LDIANASLLD EGTAAAEAMA MSFVNLRSKK RKYVVDSKLH PQSLDVIESR
ANNLGVEVVV LPLTTEEGVA QLEKIGLEVC GALVQYPATD GSLHNFSKIG EIVHKNKGLF
AMATDLLALT VLKPPAEFGA DIALGNSQRF GVPFGYGGPH AAFFATTQKF SRKVPGRIVG
VSKDRLNKPA LRLALQTREQ HIKREKATSN ICTAQALLAN MAAMYAVYHG PAGLKNIASR
VYGYTTVLAE AIKSSPHKLL NDSWFDTLSV EVNGSADALL KEALDKYNIN LFKAGESSVS
IALDETVTKS DLEGLVTLFT GKPAQLPENL PEIPQSLLRT DEILPNEVFN QHHSETAMLR
YLHLLQSKDL SLANSMIPLG SCTMKLNATV EMQTLSMPGF ALIHPFAPTD QAQGYKELIS
EFEHDLNDIT GFAATTLMPN SGAQGEYTGL SLIRQYHKAN GDYEKRNICL IPVSAHGTNP
ASAAMCGLKV VPIKCLDNGS IDITDLKDKA EKHKDNLCSI MITYPSTYGL FEPGVREAID
TVHSHGGLVY LDGANMNAQV GLTSPGDLGA DVCHLNIHKT FALSHGGGGP GQGPVCVAER
LVPYLPKHHF VDTPHATAES IQAVNSAPFG SAAVIPVSYS YIKMLGSKGL PYASALAMLN
ANYMLHRLKD QFEVLFVDPR ATKEQGTKHC AHEFIIDLRE FKSVGVEAID VAKRLQDYGF
HAPTMSFPVA GTLMIEPTES ENLEELDRFV ESMLLIRKEI DAYAKGESHG QVLKNAPHSL
ADIVSTPQEE WEARGYTREQ AAYPLPFLKT QKCWPTVARL DDAFGDMNLL CTCPSVEEVA
NEN
//
