ID A0A0A0AV73_CHAVO Unreviewed; 910 AA.
AC A0A0A0AV73;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=N301_04284 {ECO:0000313|EMBL:KGL97802.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL97802.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL97802.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL97802.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-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; KL873111; KGL97802.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0AV73; -.
DR STRING; 50402.A0A0A0AV73; -.
DR Proteomes; UP000053858; 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:UP000053858};
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..840
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:KGL97802.1"
FT NON_TER 910
FT /evidence="ECO:0000313|EMBL:KGL97802.1"
SQ SEQUENCE 910 AA; 101037 MW; 71E63B7E7F4C9D3C CRC64;
ESEILETLYN IASKNKIWRS YIGMGYYNCS VPQPIARNLL ENAGWVTQYT PYQPEVSQGR
LESLLNYQTM VCDITGMDVA NASLLDEGTA AAEAMQLCHR HNKRRKFYVD ARCHPQTIAV
VQTRANYTGV ITELKLPHEM DFSGKDVSGV LFQYPDTEGK VEDFSELVER AHQNGTLACC
ATDLLALCIL KPPGEFGVDV VLGNSQRFGV PLCYGGPHAA FFAVKENLVR MMPGRMVGVT
RDANGKEVYR LALQTREQHI RRDKATSNIC TAQALLANMA AMFGVYHGSD GLRHIARRVH
NATLILAEGL RRAGHKLHHD LFFDTLTITC GCSVKEVLDR AALRKINLRI YSDGRLGVSL
DETVNEKDLD DILWIFGCES SAELIAEGMG EETKGILSSP FKRTSKFLTH QVFNSYHSET
NIVRYMKRLE NKDISLVHSM IPLGSCTMKL NSSAELTPIS WKEFANIHPF VPLDQAQGYQ
QLFKDLEKDL CEITGYDKIS FQPNSGAQGE YAGLAAIKAY LNAKGERHRT VCLIPKSAHG
TNPASAQMAG MKIQPIEVDK NGSIDISHLK AMVDKHKENL AAIMITYPST NGVFEEEIGD
VCDLIHKHGG QVYLDGANMN AQVGLCRPGD YGSDVSHLNL HKTFCIPHGG GGPGMGPIGV
KKHLAPYLPT HPVIKIQPDK DACPLGTVSA APWGSSAILP ISWVYIKTMG AKGLKHASEI
AILNANYMAK RLEKHYKILF RGAKGKCYVA HEFILDTRPF KKTANIEAVD LAKRLQDYGF
HAPTMSWPVA GTLMIEPTES EDKAELDRFC DAMINIRQEI AEIEEGRMDP QINPLKMSPH
TLNCVTASKW DRPYSREVAA FPLPFVKPES KFWPTIARID DIYGDQHLVC TCPPMEAYES
PFSEQKRASS
//
