ID M1W6Z8_CLAP2 Unreviewed; 1063 AA.
AC M1W6Z8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=CPUR_04644 {ECO:0000313|EMBL:CCE30795.1};
OS Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE30795.1, ECO:0000313|Proteomes:UP000016801};
RN [1] {ECO:0000313|EMBL:CCE30795.1, ECO:0000313|Proteomes:UP000016801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20.1 {ECO:0000313|EMBL:CCE30795.1,
RC ECO:0000313|Proteomes:UP000016801};
RX PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA Yoshida R., Zeng Z.;
RT "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT Clavicipitaceae reveals dynamics of alkaloid loci.";
RL PLoS Genet. 9:E1003323-E1003323(2013).
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:CCE30795.1}.
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DR EMBL; CAGA01000025; CCE30795.1; -; Genomic_DNA.
DR AlphaFoldDB; M1W6Z8; -.
DR STRING; 1111077.M1W6Z8; -.
DR VEuPathDB; FungiDB:CPUR_04644; -.
DR eggNOG; KOG2040; Eukaryota.
DR HOGENOM; CLU_004620_3_1_1; -.
DR OrthoDB; 177349at2759; -.
DR PhylomeDB; M1W6Z8; -.
DR Proteomes; UP000016801; 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; 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000016801};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 84..461
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 564..842
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 879..1000
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT COILED 732..759
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 815
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1063 AA; 116433 MW; 6B38668C04C283DC CRC64;
MALRLALARG APLRPSAALL VSRAAISRAV AARWASQKTR AAPVAPLNGP HRNPFDEFRQ
DPAFGDMRMK NAEASLPWED FPTRHIGPRD EDIAAMLKQM NSGVDTLDAF VAQVIPEDIM
LPPQEKIQSL PKQYSETGIT KTFKSIHGKN IIYTWMNGGG YYPAQTPPVI KRNVFENPAW
YTSYTPYQAE VSQGRLQSLL NYQTMVCDLT GLPVANASLL DEGTAAAEAM TMSLNSLPAS
RAKRPGKTYV VSHLVHDDTI QVMRGRAEGF GIRLQVLDVS TSDAIQKIQN LGDDLIGILV
QYPDTNGGVG DYRSLADIAH KQGTLFSVAT DLSALTLLTP PGEWGADVAF GNSQRFGVPL
GFGGPHAAFM AVKESSKRRL PGRIVGVSKD RTGGRALRLA LQTREQHIRR EKATSNLCTA
QALLANMAAM YAVYHGPAQL KEMAVTNLRY SRMVQSAAQH YGLPVTTATL DPQGRVLSDT
VTITFDSAET CQTLRDNLLR NSISSGKGRA ANQVVLAAFP TFRMETYLNV VQAFKSVARK
NHSDSCVAMA NKLWTNGWKP SVKQIVDEIP DIVRRESSYL THPVFNSYHS ETEMLRYIHH
LQSKDLSLVH SMIPLGSCTM KLNATSQMEL VGYHKSSNIH PHAPESSKVG WNTLFTITRR
QLAALTGMDD TSLQPNSGAQ GEFAGLRAIR KYHEQQPGPK RDICLIPVSA HGTNPASAAM
AGMRVVPVKC DLATGNLDLA DLEAKCKQYE AELGAFMVTY PSTYGVFEPD VRKACDLVHA
HGGQVYMDGA NMNAQIGLTS PGALGADVCH LNLHKTFCIP HGGGGPGVGP ICVKSHLKPF
LPDVDGQTPV SSAAYGSASI VPISWAYMAT MGDEGLRKAT SVALLNANYL LARIKDHYPI
LYTNEKGRCA HEFIIDARPF RESAGIEAID IAKRLQDYGF HAPTMSWPVP NTLMVEPTES
ESKEELDRFA DALISIREEI REVEEGKQPR QGNVLRNAPH TQKDLIVGDG EGTWDRPYSR
QKAAYPLSYL MEKKFWPTVT RVDDTYGDTN LFCTCPPVED TTQ
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