ID A0A087QSE6_APTFO Unreviewed; 914 AA.
AC A0A087QSE6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
DE Flags: Fragment;
GN ORFNames=AS27_10714 {ECO:0000313|EMBL:KFM04150.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM04150.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM04150.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM04150.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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|RuleBase:RU364056}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000256|ARBA:ARBA00010756,
CC ECO:0000256|RuleBase:RU364056}.
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DR EMBL; KL225857; KFM04150.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087QSE6; -.
DR STRING; 9233.A0A087QSE6; -.
DR Proteomes; UP000053286; 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 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|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:UP000053286};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 1..376
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 411..670
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 717..844
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 642
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM04150.1"
FT NON_TER 914
FT /evidence="ECO:0000313|EMBL:KFM04150.1"
SQ SEQUENCE 914 AA; 101835 MW; EF7ACC1854A79976 CRC64;
ENEILETLYN CKQENKIWRS YIGMGYYNCS VPQPIARNLL ENAGWVTQYT PYQPEVSQGR
LESLLNYQTM VCDITGMDVA NASLLDEGTA AAEAMQLCHR HNKRRKFYVD ARCHPQTIAV
VQTRANYTGV ITELKLPHEM DFSGKDVSGV LFQYPDTEGR VEDFSELVER AHQNGTLACC
ATDLLALCIL KPPGEFGVDV VLGNSQRFGV PLCYGGPHAA FFAVKENLVR MMPGRMVGVT
RDANGKEVYR LALQTREQHI RRDKATSNIC TAQALLANMA AMFGVYHGSD GLRHIARRVH
NATLILAEGL RRAGHKLHHD LFFDTLTITC GCSVKEVLDR AALRKINFRI YSDGRLGVSL
DETVNEKDLD DILWIFGCES SAELIAEGMG EETKGILSTP FKRTSKFLTH QVFNSYHSET
NIVRYMKRLE NKDISLVHSM IPLGSCTMKL NSSAELTPIS WKEFANIHPF VPLDQAQGYQ
HLFKDLEKDL CEITGYDKIS FQPNSGAQGE YTGLAAIKAY LNAKGERHRT VCLIPKSAHG
TNPASAQMAG MKIQPIEVDK NGSIDISHLK AMVDKHKENL AAIMITYPST NGVFEEDIGD
VCDLIHKHGG QVYLDGANMN AQVGLCRPGD YGSDVSHLNL HKTFCIPHGG GGPGMGPIGV
KKHLAPYLPT HPVIKIQPDK DACPLGTVSA APWGSSAILP ISWVYIKTMG AKGLKHASEI
AILNANYMAK RLEKHYKILF RGARGKYWTI CYVAHEFILD TRPFKKTANI EAVDLAKRLQ
DYGFHAPTMS WPVAGTLMIE PTESEDKAEL DRFCDAMISI RQEIAEIEEG RMDPQINPLK
MSPHTLNCVT SSKWDRPYSR EVAAFPLPFV KPESKFWPTI ARIDDIYGDQ HLVCTCPPME
AYESPFSEQK RASS
//
