ID A0A0A2IG08_PENEN Unreviewed; 1057 AA.
AC A0A0A2IG08;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=PEX2_051900 {ECO:0000313|EMBL:KGO49492.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO49492.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO49492.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO49492.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO49492.1}.
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DR EMBL; JQFZ01000380; KGO49492.1; -; Genomic_DNA.
DR RefSeq; XP_016592905.1; XM_016742465.1.
DR AlphaFoldDB; A0A0A2IG08; -.
DR STRING; 27334.A0A0A2IG08; -.
DR GeneID; 27677884; -.
DR HOGENOM; CLU_004620_3_2_1; -.
DR OrthoDB; 177349at2759; -.
DR PhylomeDB; A0A0A2IG08; -.
DR Proteomes; UP000030143; 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; 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 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:UP000030143};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 75..536
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 554..825
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 878..999
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 37..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 802
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1057 AA; 115136 MW; 5313BD616856386C CRC64;
MAASLFALRG GRQLALRSRV RVPTIARASL SPLNTRRALN TSQPATRRGV YTSSISDHGD
PHPQDIFQPL DTFPRRHIGP SPEAAAQMLA VLDPPVASLD DFVKQVLPED ILSKKDLKVS
EPHADISLYR SSVQGGLGET DMLKLLDTYR KQIDISGKTY IGTGYYPTIV PPVIQRNVLE
NPAWYTSYTP YQPEISQGRL ESLLNFQTLT ADLTGLPFAN ASVLDEATAA AEAMTMSFAT
MPASKQKKAD KSFVVSHLCH PQTIAVMRSR AEGFGINLVI GDILADDFKI VKDQKDHLIG
VLAQYPDTEG GIYEFQALSD SIHGQGGTFS VATDLLALTV LKAPGEFGAD IAFGSAQRLG
VPMGFGGPHA AFFACADKYK RKVPGRVVGV SKDRLGNRAL RLALQTREQH IRREKATSNI
CTAQALLANM TAMYAIYHGP VGLKSIAQRI MSMTSLLREK LVSLGYDVPV RSNSADGGAV
FDTLAIELSS AAEADAIMAE ARAASVFLRR LGGNKVGLSL DETVGRDEVK GILNVFAAHK
SASPVEVDGT LGLTTVPASL ERTSSYLTHP VFNTYHSETE MLRYIHHLES KDLSLAHSMI
PLGSCTMKLN ATTEMIPVSW PEFSQIHPFM PAEQAKGYTK MIDDLEQQLA DITGMAEVTV
QPNSGAQGEF AGLRVIKKYF EAKGDAKRNL CLIPVSAHGT NPASAAMAGM RVVTVKCDTK
TGNLDLEDLK AKCEKHKDEL AAFMITYPST FGVFEPGAKE ACRLVHQHGG QVYMDGANMN
AQIGLCSPGE IGADVCHLNL HKTFCIPHGG GGPGVGPIGV GEHLRPFLPS HPTSEYLQSK
RGDTSSPPIS AAPWGSASIL PITFNYINMM GDRGLTHATK ITLLNANYIL SRLKPYYSIL
YTNDHGRCAH EFILDVRAFK ETCGVEAIDI AKRLQDYGFH APTMSWPVSN TLMIEPTESE
NKAELDRFCD ALISIRKEIS EVESGAQPRE GNVLKMSPHT QRDLLTSEWD RPYTREQAAY
PLPLLLEKKF WPTVTRVDDA FGDQNLFCTC GPVEDTE
//
