ID A0A077S2R7_WHEAT Unreviewed; 1031 AA.
AC A0A077S2R7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=CFC21_041748 {ECO:0000313|EMBL:KAF7030142.1},
GN TRAES_3BF092100100CFD_c1 {ECO:0000313|EMBL:CDM83805.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EMBL:CDM83805.1};
RN [1] {ECO:0000313|EMBL:CDM83805.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25035497; DOI=10.1126/science.1249721;
RA Choulet F., Alberti A., Theil S., Glover N., Barbe V., Daron J.,
RA Pingault L., Sourdille P., Couloux A., Paux E., Leroy P., Mangenot S.,
RA Guilhot N., Le Gouis J., Balfourier F., Alaux M., Jamilloux V., Poulain J.,
RA Durand C., Bellec A., Gaspin C., Safar J., Dolezel J., Rogers J.,
RA Vandepoele K., Aury J.M., Mayer K., Berges H., Quesneville H., Wincker P.,
RA Feuillet C.;
RT "Structural and functional partitioning of bread wheat chromosome 3B.";
RL Science 345:1249721-1249721(2014).
RN [2] {ECO:0000313|EMBL:KAF7030142.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7030142.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS3B02G279700.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS3B02G279700.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [4] {ECO:0000313|EnsemblPlants:TraesCS3B02G279700.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [5] {ECO:0000313|EMBL:KAF7030142.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7030142.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) 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|ARBA:ARBA00004173,
CC 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; HG670306; CDM83805.1; -; Genomic_DNA.
DR EMBL; CM022218; KAF7030142.1; -; Genomic_DNA.
DR SMR; A0A077S2R7; -.
DR STRING; 4565.A0A077S2R7; -.
DR EnsemblPlants; TraesCS3B02G279700.1; TraesCS3B02G279700.1; TraesCS3B02G279700.
DR Gramene; TraesCS3B02G279700.1; TraesCS3B02G279700.1; TraesCS3B02G279700.
DR Gramene; TraesCS3B03G0721900.1; TraesCS3B03G0721900.1.CDS; TraesCS3B03G0721900.
DR Gramene; TraesKAR3B01G0305440.1; cds.TraesKAR3B01G0305440.1; TraesKAR3B01G0305440.
DR Gramene; TraesWEE_scaffold_003837_01G000500.1; TraesWEE_scaffold_003837_01G000500.1; TraesWEE_scaffold_003837_01G000500.
DR HOGENOM; CLU_004620_3_2_1; -.
DR OMA; DEHCHPQ; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000019116; Chromosome 3B.
DR Proteomes; UP000815260; Chromosome 3B.
DR ExpressionAtlas; A0A077S2R7; baseline and differential.
DR GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0016594; F:glycine binding; IBA:GO_Central.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
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 HAMAP; MF_00711; GcvP; 1.
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|ARBA:ARBA00023128,
KW 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:UP000019116};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1031
FT /note="Glycine cleavage system P protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039969263"
FT DOMAIN 73..500
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 518..793
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 844..965
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 19..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 766
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1031 AA; 111045 MW; 1A5E76664932516E CRC64;
MERARRLASR ALLRRLLAAS SSATSPAPSR GVSTLAPKPA AGSRPRARPA HQYTPGRPVS
VSALQPSDTF PRRHNSATPA EQAVMASECG FNTLDALIDA TVPAAIRAPP MQFTGKFDAG
FTESQMLEHM AHLASMNKTY KSFIGMGYYN THIPAVILRN LMENPAWYTQ YTPYQAEIAQ
GRLESLLNYQ TMVADLTGLP MSNASLLDEA TAAAEAMAMC LGIVKSKKKT FLIASNCHPQ
TIDICQTRAT GFDINVVVSA AKDFDYSSGD VCGVLVQYPG TEGEVLDYAE FVKDAHAHGV
KVVMATDLLA LTTLRPPGEI GADIAVGSAQ RFGVPMGYGG PHAAFLATSQ EYKRLMPGRI
IGVSVDSSGK PALRMAMQTR EQHIRRDKAT SNICTAQALL ANMAAMYAVY HGPAGLKAIA
DRVHGLAGTF AHGLKKLGTV TVQELPYFDT VKITCADANA IAEEARKSEM NLRVVDANTI
TVAFDETTTL EDVDKLFKVF SGGKPVDFTA ESIAPEVSSS IPPSLVRDSP YLTHPIFSMY
HTEHELLRYL HKLQSKDLSL CHSMIPLGSC TMKLNATVEM MPVTDPKFAN MHPFAPIDQA
AGYHEMFDNL GDLLNTITGF DSFSLQPNAG ASGEYAGLMV IRAYHKARGD HHRNVCIIPV
SAHGTNPASA AMCGMKIVAV GTDAKGNINI EELRKAAEAN KDNLSALMVT YPSTHGVYEE
GIDEICRIIH ENGGQVYMDG ANMNAQVGLT SPGFIGADVC HLNLHKTFCI PHGGGGPGMG
PIGVKKHLAP FLPSHPVIPT GGFPLPEKTD PLGSISAAPW GSALILPISY TYIAMMGSQG
LTEASKIAIL NANYMAKRLE KHYPVLFRGV NGTVAHEFII DLRGFKATAG IEPEDVAKRL
MDYGFHGPTM SWPVPGTLMI EPTESESKAE LDRFCDALIS IREEIAQVEN GKADAHNNVL
KGAPHPPQLL MGDAWTKPYS REYAAFPAAW LRGAKFWPTT CRVDNVYGDR NLICTLQQAS
QVAEEAAAAT A
//
