ID A0A0S3RPJ3_PHAAN Unreviewed; 1062 AA.
AC A0A0S3RPJ3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN Name=Vigan.03G254300 {ECO:0000313|EMBL:BAT82514.1};
GN ORFNames=VIGAN_03254300 {ECO:0000313|EMBL:BAT82514.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT82514.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT82514.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(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|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 EMBL; AP015036; BAT82514.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3RPJ3; -.
DR Proteomes; UP000291084; 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; 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:UP000291084};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 105..531
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 544..824
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 875..996
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 797
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1062 AA; 115372 MW; 15CC1A8A045FE575 CRC64;
MERARRLANR AILKRLVSEA KQHQKNESLL HSSTTPMLLY SSSRCMSSVS SAAVRNRGFK
TETLLGRSMN IATMSRGVVG GLLGVGSTRS ISVEALQRSD TFPRRHNSAT PEEQSKMAES
IGFESLDSLV DATVPKSIRL KEMKFGKFDG GLTESQMIEH MKDLASKNKV FKSYIGMGYY
NTHVPPVILR NIMENPAWYT QYTPYQAEIS QGRLESLLNY QTMITDLTGL PMSNASLLDE
GTAAAEAMSM CNNIQKGKKK TFIIASNCHP QTIDICKTRA AGFDLKVVTA DLKDIDYKSG
DVCGVLVQYP GTEGEVLDYG EFIKKAHAHE VKVVMASDLL ALTVLKPPGE LGADIVVGSA
QRFGVPMGYG GPHAAFLATS QEYKRMMPGR IIGVSVDSTG KTALRMAMQT REQHIRRDKA
TSNICTAQAL LANMAAMYAV YHGPEGLKNI ANRVHGLAGA FALGLKKLGT VEVQDLPFFD
TVKVKTSNAH AIADAAIKSE INLRVVDGNT ITVAFDETTT LEDVDKLFKV FAGGKPVPFT
AASIASEVQS AIPSGLTRNS PYLTHPIFNT YQTEHELLRY MYRLQSKDLS LCHSMIPLGS
CTMKLNATTE MMPVTWSNFS DIHPFAPVNQ AEGYQEMFDN LGDLLCTITG FDSFSLQPNA
GAAGEYAGLM VIRAYHLARG DHHRDVCIIP VSAHGTNPAS AAMCGMKIVS VGTDAKGNIN
IEELRKAAEK HKDNLSALMV TYPSTHGVYE EGIDEICKII HDNGGQVYMD GANMNAQVGL
TSPGWIGADV CHLNLHKTFC IPHGGGGPGM GPIGVKKHLA PFLPSHPVIS TGGIPAPENP
QPLGTISAAP WGSALILPIS YTYIAMMGSK GLTDASKIAI LNANYMAKRL ENYYPVLFRG
VNGTVAHEFI IDLRGFKNTA GIEPEDVAKR LMDYGFHAPT MSWPVPGTLM IEPTESESKA
ELDRFCDTLI SIREEIAEIE KGKADINNNV LKGAPHPPSL LMADAWTKPY SREYAAFPAP
WLRASKFWPT TGRVDNVYGD RNLICTLLPA SQAVEEEAAA TA
//
