ID G0P9Z1_CAEBE Unreviewed; 979 AA.
AC G0P9Z1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=CAEBREN_00815 {ECO:0000313|EMBL:EGT48156.1}, CAEBREN_17799
GN {ECO:0000313|EMBL:EGT48793.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|EMBL:EGT48793.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PB2801 {ECO:0000313|EMBL:EGT48793.1};
RG The Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:EGT48793.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|EMBL:EGT48793.1};
RG WormBase Consortium;
RL Submitted (JUL-2011) 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; GL379822; EGT48156.1; -; Genomic_DNA.
DR EMBL; GL380162; EGT48793.1; -; Genomic_DNA.
DR STRING; 135651.G0P9Z1; -.
DR EnsemblMetazoa; CBN00815.1; CBN00815.1; WBGene00139540.
DR EnsemblMetazoa; CBN17799.1; CBN17799.1; WBGene00156524.
DR eggNOG; KOG2040; Eukaryota.
DR HOGENOM; CLU_004620_3_2_1; -.
DR OMA; RNLICTC; -.
DR Proteomes; UP000008068; 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|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:UP000008068};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 32..462
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 503..760
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 802..922
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 731
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 979 AA; 108992 MW; EA73303FA15B45C1 CRC64;
MVLFGRGLLA AGRLALRRPT IARHLQYDAF VDRHIGPRRL EQQQMLDFIG YKDLDDLTGT
NVPNMIKIEK ALELPAPLDE YKMLKELEAI AAQNKIYRSY IGMGYYDTIV PAVISRNILQ
NIGWISQYTP YQAEISQGRL ESLLNFQTMI AEMTGLPTTN ASLLDEATAS AEAVALAART
TKRNKVIVDS FCHPQNLDVI KTRSDPLGIS IEVCDAVESF EFDDKVAAVV VQYPNTEGRI
HQFDELIEKA HKNNSLVIMV CDLLSLTILR SPGDLGADIA VGSAQRFGVP LGYGGPHAGF
MAVAKHDAKN ALGRNMPGRI IGVTKDANGN RALRLALQTR EQHIRRDKAT SNICTAQALL
ANMSAMYAVY HGPQRLTEIA RGVHKSTAYL AYHLRNAGHE IVHKDYFDTL KVRLKNGEAL
EELKKRAEEM KMNFRYYENG DVGVSLDETV KSEDLMDIIY TFNGHTEKDV TKLREERWEV
ACPLIGNSPH SRSSLFLQHP VFNTYHSEQQ LVRYMKRLEN KDVSLVHSMI PLGSCTMKLN
ASAELIPITW PTLSSIHPFA PIEQAKGYSQ IFGDLEKWLC EITGYDNFSL QPNSGANGEY
AGLLAIRNYL IHKGQEQRNI CLIPTSAHGT NPASAQMANM KVVVVDSDHH GNINYKDLAA
KAEKYSNQLA AIMVTYPSTH GVFESSIRDV CDKVHEHGGQ VYLDGANMNA QVGLCRPGDY
GSDVSHLNLH KTFCIPHGGG GPGVGPIGVK KHLAPFLPGH SVIPVDGRRG GSVASAPYGS
ASILAITWAY IRMMGGNGLR EASQVAILNA NYMAKRLENE YRIVYKDEQG LVAHEFIMDC
KPFKKHGIEV VDIAKRLMDY GFHSPTMSWP VHDCLMIEPT ESEDKGEMDR LVDALLAIRE
EIRQVENGTF DKHLNPLKMA PHTLEKVISD TWNMPYSREL AAFPKPWCAH KAWPTVGRVD
DQYGDRNLVC TCPPIESYQ
//
