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Database: UniProt
Entry: A0A2K5EMA3_AOTNA
LinkDB: A0A2K5EMA3_AOTNA
Original site: A0A2K5EMA3_AOTNA 
ID   A0A2K5EMA3_AOTNA        Unreviewed;       997 AA.
AC   A0A2K5EMA3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE            EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN   Name=GLDC {ECO:0000313|Ensembl:ENSANAP00000034311.1};
OS   Aotus nancymaae (Ma's night monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000034311.1, ECO:0000313|Proteomes:UP000233020};
RN   [1] {ECO:0000313|Ensembl:ENSANAP00000034311.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:ARBA00033655,
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}.
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DR   AlphaFoldDB; A0A2K5EMA3; -.
DR   Ensembl; ENSANAT00000052375.1; ENSANAP00000034311.1; ENSANAG00000034753.1.
DR   GeneTree; ENSGT00390000017970; -.
DR   Proteomes; UP000233020; Unplaced.
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; 1.
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; 1.
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:UP000233020};
KW   Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT   DOMAIN          65..488
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          806..927
FT                   /note="Glycine dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21478"
FT   MOD_RES         733
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ   SEQUENCE   997 AA;  110579 MW;  FAC8F1B6BDE2C5F8 CRC64;
     MQSCARAWGL RLGRGVGGCR RLAGGSGPCW APRGRDSSSG GGDDAAAGAS RLLERLLPRH
     DDFARRHIGP GDKDQKEMLQ TLGLASIDEL IEKTVPASIR LKRPLKMEDP VCENEILATL
     HAISSKNQIW RSYIGMGYYN CSVPQTILRN LLENSGWITQ YTPYQPEVSQ GRLESLLNYQ
     TMVCDITGLD MANASLLDEG TAAAEALQLC YRHNKRRKFF VDPRCHPQTI AVVQTRAKYT
     GVLIELKLPH EMDFSGKDVS GVLFQYPDTE GKVEDFTELV ERAHQSGSLA CCATDLLALC
     ILRPPGEFGV DIALGSSQRF GVPLGYGGPH AAFFAVRESL VRMMPGRMVG VTRDATGKEV
     YRLALQTREQ HIRRDKATSN ICTAQALLAN MAAMFAIYHG SRGLEHIARR VHNATLILSE
     GLKRAGHQLQ HDLFFDTLKI QCGCSVKEVL GRAAQRQINF RLFEDGTLGI SLDETVNEKD
     LDDLLWIFGC ESSAELVAES MGEERRGIPG SVFKRTSQFL THQVFNSYHS ETNIVRYMKK
     LENKDISLVH SMIPLGSCTM KLNSSSELTP ITWKEFANIH PFVPLDQAQG YQQLFRELEK
     DLCELTGYDR ISFQPNSGAQ GEYAGLATIR AYLDQKGEGH RTVCLIPKSA HGTNPASAHM
     AGMKIQPVEV DKDGNIDAAH LKAMVDKHKE NLAAIMIRTH PPMGLPRRAN MNAQVGTGES
     TLGDDVSHLN LHKTSAFPTG GGPAWGPSEK KHLAPFLPNH PIISLKLNED TRPVGTISAA
     PWGSSSILPI SWAYIKMMGG KGLKQATETA ILNANYMAKR LEKHYRILFR GARGYVGHEF
     ILDTRPFKKS ANIEAVDVAK RLQDYGFHAP TMSWPVAGTL MVEPTESEDK AELDRFCDAM
     ISIRQEIADI EEGRIDPRVN PLKMSPHSLT CVTSSHWDRP YSREVAAFPL PFVKPENKFW
     PTIARIDDIY GDQHLVCTCP PMEVYESPFS EQKRASS
//
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