ID G2WWU8_VERDV Unreviewed; 1068 AA.
AC G2WWU8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=VDAG_02727 {ECO:0000313|EMBL:EGY21203.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY21203.1, ECO:0000313|Proteomes:UP000001611};
RN [1] {ECO:0000313|Proteomes:UP000001611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC {ECO:0000313|Proteomes:UP000001611};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
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; DS572698; EGY21203.1; -; Genomic_DNA.
DR RefSeq; XP_009651675.1; XM_009653380.1.
DR AlphaFoldDB; G2WWU8; -.
DR STRING; 498257.G2WWU8; -.
DR EnsemblFungi; EGY21203; EGY21203; VDAG_02727.
DR GeneID; 20704190; -.
DR KEGG; vda:VDAG_02727; -.
DR eggNOG; KOG2040; Eukaryota.
DR HOGENOM; CLU_004620_3_2_1; -.
DR InParanoid; G2WWU8; -.
DR OMA; RNLICTC; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000001611; Chromosome 3.
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:UP000001611};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 87..530
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 584..839
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 877..998
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 810
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1068 AA; 115976 MW; CFAD01C2341F609E CRC64;
MASTRLPLPR HLRLRVASPR FTSGLTRASP ASSARVASLC ARPATAASLP IGIRAFSATS
SALTPYAKDN TDASLEPLNE IHTFIPRHIG PDIHDAQQML KALDPPVKTI DEFIAEVIPA
DILSERASFL PNGEPLLESD IASIAKMLKT TEQYAAPLIG AGYYPTITPQ VIQTNVLENP
AWYTSYTPYQ PEISQGRLES LLNFQTMVSD LTALPISNAS LLDEGTAAAE AMTLSMNALT
TSRAKRAGKT YVVSHQIHPQ TLSVLQGRSQ GFGIKIETMD VTSPDAHERI KALGDDLVGV
MVQYPDTRGH VEDFKALSEV VHSQKALLAV ATDLLALTLI TPPGEWGADI AFGTAQRFGI
PLGFGGPHAA FFSVTDAHKR RMPGRLIGVS RDRTGKNAMR LSLQTREQHI RREKATSNVC
TAQALLANMS ALYAIYHGPE GLKQIANQVV ARARGVQALA KQFGITTEEP RNSPDGKVLF
DTVILKAGDT LAENIVEKGE QLGLHFRKLG SGDLGVSIGE ATDAQAFQRL AITFAAATGG
DPNTAGDAAI EVLRKEGVDV HSTLPDTFKR QSEYLTHPVF NTHRSETEIL RYIYHLQSKD
LSLVHSMIPL GSCTMKLNGA TEMSLISKDT FSNPHPFVDP KHTPAYLEFI KQLEDQLSGI
TAMDATTLQP NSGAQGEFAG LRAIRRYHEQ QPGTKRDICL IPKSAHGTNP ASAAMAGMRV
VPIECDNLTG NLDIADLEAK CKKHAAELGA IMVTYPSTYG VFEPNIKQVC NIVYEHGGQV
YMDGANMNAQ IGLCSPGEIG ADVCHLNLHK TFCIPHGGGG PGVGPICVKK HLAPYLPGRH
PDDKEAMISS APYGSAGILP IPWAYNSLMG NRGLALATKM AILNANYLLA RLKPYYKILY
TNEGGRCAHE FILDARPFSK TAGIEVIDIA KRLQDYGFHS PTMSWPVANT LMIEPTESES
KEELDRFVDA LISIRAEIRE IEEGKQPREG NVLKMAPHPQ ADVILGDNGK WERPYSREQA
AYPLPWLKEK KFWPSVARVD DAFGDTNLFC TCPPVADTTG EQSFGVQA
//
