ID A0A3S3MZQ8_9MAGN Unreviewed; 1048 AA.
AC A0A3S3MZQ8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=CKAN_00656500 {ECO:0000313|EMBL:RWR78056.1};
OS Cinnamomum micranthum f. kanehirae.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Cinnamomum.
OX NCBI_TaxID=337451 {ECO:0000313|EMBL:RWR78056.1, ECO:0000313|Proteomes:UP000283530};
RN [1] {ECO:0000313|EMBL:RWR78056.1, ECO:0000313|Proteomes:UP000283530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chaw 1501 {ECO:0000313|Proteomes:UP000283530};
RC TISSUE=Young leaves {ECO:0000313|EMBL:RWR78056.1};
RX PubMed=30626928; DOI=10.1038/s41477-018-0337-0;
RA Chaw S.M., Liu Y.C., Wu Y.W., Wang H.Y., Lin C.I., Wu C.S., Ke H.M.,
RA Chang L.Y., Hsu C.Y., Yang H.T., Sudianto E., Hsu M.H., Wu K.P., Wang L.N.,
RA Leebens-Mack J.H., Tsai I.J.;
RT "Stout camphor tree genome fills gaps in understanding of flowering plant
RT genome evolution.";
RL Nat. Plants 5:63-73(2019).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RWR78056.1}.
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DR EMBL; QPKB01000002; RWR78056.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S3MZQ8; -.
DR STRING; 337451.A0A3S3MZQ8; -.
DR Proteomes; UP000283530; 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 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:UP000283530};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 91..517
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 535..810
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 861..982
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 20..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 783
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1048 AA; 113533 MW; 0B0977780BF3B123 CRC64;
MERARRLATR AILRRLISES KRSHLAHSSS PSPLSSFPSS SRFISSLSPS IFSSSDQKNA
VAAAASTSAL RSQSRSISVE ALKPSDTFPR RHNSATPEEQ KKMAESCGFP TLDSLIDATV
PKSIRISGME FSKFDEGLTE SQMIAHMKSL ASKNRVFKSY IGMGYYDTYV PAVILRNIME
NPGWYTQYTP YQAEIAQGRL ESLLNFQTLI TDLTGLPMSN ASLLDEGTAA AEAMAMCNNI
QRGKKKTFVI ASNCHPQTID ICKTRADGFN LKVVTADLKD FDYSSNDVCG VLVQYPGTEG
EVLDYGEFIK NAHAKGVKVV MASDLLALTM LKPPGELGAD IVVGSAQRFG VPMGYGGPHA
AFLATSQEYK RMMPGRIIGV SVDSSGKPAL RMAMQTREQH IRRDKATSNI CTAQALLANM
AAMYAVYHGP DGLKVIAERV HGLAGVFALG LKKLGTVEVQ GLPFFDTVKI KCANSQAIAD
AACKSGINLR IVDSKTITVS FDETTTLEDV DELFKVFAGG KSVTFTAAAL APEVQSTIPH
GLVRESPYLT HPIFNMYHTE HELLRYIHKL QSKDLSLCHS MIPLGSCTMK LNATAEMMPV
TWPEFANIHP FAPTEQAMGY QEMFEDLGEL LCTITGFDSF SLQPNAGAAG EYAGLMVIRA
YHVARGDHHR DVCIIPVSAH GTNPASAAMC GMKIVSVGTD AKGNINIEEL RKAAEANKGN
LSALMVTYPS THGVYEEGID EICKIIHDNG GQVYMDGANM NAQVGLTSPG WIGADVCHLN
LHKTFCIPHG GGGPGMGPIG VKKHLAPFLP SHPVVPTGGI PPPEKFQPLG TISAAPWGSA
LILPISYTYV AMMGSKGLTE ASKIAILNAN YMAKRLENYY PILFRGVNGT VAHEFIVDLR
GFKNTAGIEP EDVAKRLMDY GFHGPTMSWP VPGTLMIEPT ESESKAELDR FCDALISIRE
EIAQIESGKA DIKDNVLKGA PHPASLLMGD TWTKPYSREY AAFPAAWLRS AKFWPTTGRV
DNVYGDRNLT CTLLPASHYV EEEAAATA
//
