ID A0A061HII3_BLUGR Unreviewed; 1058 AA.
AC A0A061HII3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=BGT96224_795 {ECO:0000313|EMBL:EPQ66005.1},
GN BGT96224V2_LOCUS2229 {ECO:0000313|EMBL:SUZ09061.1};
OS Blumeria graminis f. sp. tritici 96224.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria.
OX NCBI_TaxID=1268274 {ECO:0000313|EMBL:SUZ09061.1};
RN [1] {ECO:0000313|Proteomes:UP000053110}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=96224 {ECO:0000313|Proteomes:UP000053110};
RX PubMed=23852167; DOI=10.1038/ng.2704;
RA Wicker T., Oberhaensli S., Parlange F., Buchmann J.P., Shatalina M.,
RA Roffler S., Ben-David R., Dolezel J., Simkova H., Schulze-Lefert P.,
RA Spanu P.D., Bruggmann R., Amselem J., Quesneville H.,
RA Ver Loren van Themaat E., Paape T., Shimizu K.K., Keller B.;
RT "The wheat powdery mildew genome shows the unique evolution of an obligate
RT biotroph.";
RL Nat. Genet. 45:1092-1096(2013).
RN [2] {ECO:0000313|EMBL:EPQ66005.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=96224 {ECO:0000313|EMBL:EPQ66005.1};
RA Oberhaensli S., Wicker T., Keller B.;
RT "The wheat powdery mildew genome reveals unique evolution of an obligate
RT biotroph.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SUZ09061.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=96224 {ECO:0000313|EMBL:SUZ09061.1};
RA Quirk P.G., Krulwich T.A.;
RL Submitted (JUL-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 ---------------------------------------------------------------------------
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; KE375011; EPQ66005.1; -; Genomic_DNA.
DR EMBL; UIGY01000038; SUZ09061.1; -; Genomic_DNA.
DR HOGENOM; CLU_004620_3_2_1; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000053110; 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; 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:UP000053110};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 78..532
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 561..836
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 MOD_RES 807
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1058 AA; 116034 MW; 13AB4D35B316A3FA CRC64;
MAASALAIRA QLGRVARYYG NSSKSLRQSR QTLSRNSALK VCAKYPNVNL RTFHNNSAES
PRPPTNSESH LPLDTFARRH IGPSEDSIQE MLKALDPPVE SLDEFVKQVL PADILSSKNL
KIDTKQSAHG DAFTESEVLE ILRKKMENEE FKSVRTFIGC GYTNTIVPEV IKRNVLEGPG
WYTSYTPYQP EISQGRLESL LNFQTLVSDL TALPISNASL LDEATAAAEA MTLSMNVSPS
SKHKNPNKTF FVSHLVHPQT KAVIQSRADG FGIKIVFGDA LANDGEEIKN IGADLIGALV
QYPDTEGGVE DFKGLAEIIH QQGAIFSVAT DLLALTVLTP PGEFGADIAF GSSQRLGVPL
GFGGPHAAFF AVNDKLKRRI PGRLIGISKD RSGKKALRLA LQTREQHIRR EKATSNVCTA
QALLANMSAF YAIYHGPDGL KNIAEKIITS ARSLEDGLRV LGLETGTRGK GKDGKVLFDT
VVVQVPGRAR EIQNLALSTQ KINLRLFDED RIGITVDESV NASDLKDILS IFSLHMKNHG
KSSADADKMI ESAFKKQSLD IPSVLKRSSK YLTHPVFNSY HSETEILRYI HHLQSKDLSL
THSMIPLGSC TMKLNSTSEM IPVSWPEFSN VHPFVPENQT KGYRSIINEL ETDLSELTGF
DAVSLQPNSG AQGEFTGLRV ISRYQQEKSG KKRDVCLIPV SAHGTNPASA TMAGMRVVTV
KCDTSTGNLD LADLKAKCEK YSDELSAIMV TYPSTFGVFE PEIKQVCKLV HEHGGQVYMD
GANMNAQIGL CTPGDIGADV CHLNLHKTFC IPHGGGGPGV GPIGVKAHLA PFLPGHPIIK
TGGENAIAPV SGAPFGSASI LPISWTYIKM MGGRGLTHAT KVTLLNANYI MSRLRPHYPI
LYTNSNLRCA HEFILDARGF KETCKIEAID IAKRLQDYGF HGPTMSWPVA NTLMIEPTES
ESKAELDRFI DALISIRAEI RDIEEGRVSK EMNVMKMSPH TQADLIIGEW DRPYSREQAA
YPLPWLKEKK FWPTVTRIDD AYGDTNLFCT CPPVEPTD
//
