ID A0A1U8JHE2_GOSHI Unreviewed; 1050 AA.
AC A0A1U8JHE2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 08-OCT-2025, sequence version 2.
DT 28-JAN-2026, entry version 40.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN Name=LOC107907004 {ECO:0000313|RefSeq:XP_016689681.2};
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000818029, ECO:0000313|RefSeq:XP_016689681.2};
RN [1] {ECO:0000313|Proteomes:UP000818029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000818029};
RX PubMed=32313247; DOI=10.1038/s41588-020-0614-5;
RA Chen Z.J., Sreedasyam A., Ando A., Song Q., De Santiago L.M.,
RA Hulse-Kemp A.M., Ding M., Ye W., Kirkbride R.C., Jenkins J., Plott C.,
RA Lovell J., Lin Y.M., Vaughn R., Liu B., Simpson S., Scheffler B.E., Wen L.,
RA Saski C.A., Grover C.E., Hu G., Conover J.L., Carlson J.W., Shu S.,
RA Boston L.B., Williams M., Peterson D.G., McGee K., Jones D.C., Wendel J.F.,
RA Stelly D.M., Grimwood J., Schmutz J.;
RT "Genomic diversifications of five Gossypium allopolyploid species and their
RT impact on cotton improvement.";
RL Nat. Genet. 52:525-533(2020).
RN [2] {ECO:0000313|RefSeq:XP_016689681.2}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. {ECO:0000256|RuleBase:RU364056}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage complex H protein]
CC + glycine + H(+) = N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-L-lysyl-
CC [glycine-cleavage complex H protein] + CO2; 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:ARBA00049026,
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: Homodimer. The glycine cleavage system is composed of four
CC proteins: P, T, L and H. {ECO:0000256|ARBA:ARBA00046415}.
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}.
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DR RefSeq; XP_016689681.2; XM_016834192.2.
DR AlphaFoldDB; A0A1U8JHE2; -.
DR SMR; A0A1U8JHE2; -.
DR STRING; 3635.A0A1U8JHE2; -.
DR PaxDb; 3635-A0A1U8JHE2; -.
DR GeneID; 107907004; -.
DR KEGG; ghi:107907004; -.
DR Proteomes; UP000818029; Chromosome D05.
DR GO; GO:0048046; C:apoplast; IEA:TreeGrafter.
DR GO; GO:0009941; C:chloroplast envelope; IEA:TreeGrafter.
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 NCBIfam; NF003346; PRK04366.1; 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|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR603437-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000818029};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 93..519
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 536..812
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 863..984
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 14..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 785
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1050 AA; 114015 MW; 6C033CB19C9A694E CRC64;
MERARKVANR AILKRLVNES KQSRNGEMSS RSPVSYTPSR YVSSLSPFGS KNHSRSDSLG
ARNVSNNVGF GVGSPIRSIS VEALKSSDTF PRRHNSATPE EQTKMAESCG FDSLDALIDA
TVPKAIRIDS MKFPKFDGGL TESQMIEHMK DLESKNKIFK SFIGMGYYNT HVPPVILRNI
MENPAWYTQY TPYQAEISQG RLESLLNFQT MITDLTGLPM SNASLLDEGT AAAEAMAMCN
NIVKGKKKTF IIANNCHPQT IDICKTRADG FDLKVVTADL KDIDYSSGDV CGVLVQYPGT
EGEILDYGEF VKNAHAQGVK VVMATDLLAL IMLKPPGELG ADIVVGSAQR FGVPMGYGGP
HAAFLATSQE YKRMMPGRII GVSVDSSGKP ALRMAMQTRE QHIRRDKATS NICTAQALLA
NMAAMYAVYH GPEGLKTIAQ RVHGLAGAFA VGLKKLGNIE VQGLPFFDTV KVTCADAHAI
ADAAYKSEIN LRVVDAKTIT VSFDETTTLD DLDKLFKVFA GGKPVSFTAA SLAPEVENAI
PSGLLRQSSY LTHQIFNMYH TEHELLRYLH KLQSKDLSLC HSMIPLGSCT MKLNATTEMM
PVTWPGFTDI HPFAPSEQAQ GYQEMFNNLG DLLCTITGFD SFSLQPNAGA AGEYAGLMVI
RAYHKSRGDH HRNVCIIPVS AHGTNPASAA MCGMKIVPVG TDSKGNINIE ELRKAAEANR
DKLSALMVTY PSTHGVYEEG IDEICRIIHD NGGQVYMDGA NMNAQVGLTS PGFIGADVCH
LNLHKTFCIP HGGGGPGMGP IGVKKHLAPF LPSHPVVSTG GIPAPDKSHP LGTISAAPWG
SALILPISYT YIAMMGSKGL TDASKIAILN ANYMAKRLEN YYPVLFRGVN GTVAHEFIVD
LRGFKNTAGI EPEDVAKRLM DYGFHGPTMS WPVPGTLMIE PTESESKAEL DRFCDALISI
REEIAQIENG KADIHNNVLK GAPHPPSLLM GDAWTKPYTR EYAAFPASWL RTAKFWPTTG
RVDNVYGDRN LICTLLPVSQ MVEEEAAANA
//
