ID A0A3P8T2H6_AMPPE Unreviewed; 1032 AA.
AC A0A3P8T2H6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000018433.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000018433.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000018433.1}
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: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 AlphaFoldDB; A0A3P8T2H6; -.
DR STRING; 161767.ENSAPEP00000018433; -.
DR Ensembl; ENSAPET00000018942.1; ENSAPEP00000018433.1; ENSAPEG00000013111.1.
DR GeneTree; ENSGT00390000017970; -.
DR OMA; RNLICTC; -.
DR Proteomes; UP000265080; Chromosome 5.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
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; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
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; PF01212; Beta_elim_lyase; 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:UP000265080};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 78..501
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 599..742
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT DOMAIN 842..963
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 767
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1032 AA; 114477 MW; 78F428E42AE6F962 CRC64;
MQSCARSWGI FLAKSVNPGA PCRHLSDKSR VVWKLQCRNP NTCASLTTAA AVRGVRTSAA
LSSRQIERIL PRHDDFAERH IGPGEREKRE MLDVLGLESV DQLIEDTVPS SIRMQRSMKM
DDPVCENEVL ESLQKIASKN KVWRSYIGMG YYNCSVPPPI QRNLLENAGW VTQYTPYQPE
VSQGRLESLL NYQTMICDIT GMPVANASLL DEGTAAAEAM QLCHRQNKRR TFYIDPRCHP
QTIAVVQTRA NYIGVKTELK LPHEMDFSGK DVSGVLFQYP DTDGRVEDFT ALVDRAHKGG
ALACCATDLL ALCVLRPPGE FGVDIALGSS QRFGVPLCYG GPHAAFFAVR DNLVRMMPGR
MVGVTRDAAG KEVYRLALQT REQHIRRDKA TSNICTAQAL LANMAAMYTL YHGPQGLKHI
AERTHNAALI LAEGLKRAGH RLHSDMFFDT LKINCSVAAK DILERAVQRE INLRVYTEGV
LGVSLDETVT ERDLDDLLWV FGCESSAELI AEKMGERVKG IMGSPFKRTS KYLTHQVFNS
YHSETNIVRY MKRLENKDIS LVHSMIPLGS CTMKLNSSSE LMPITWREFG NIHPFVPLDQ
AEGYQKLFRQ LEKDLCEVTG YDKISFQPNS GAQGEYAGLA AIKAYLNSKG ESSRSVCLIP
KSAHGTNPAS AQMAGMKVQV VEVDKDGNID LSHLKALVDK HKASLAAMMI TYPSTFGVFE
ERIRDVCDLI HSNGGQVYLD GANMNAQVGL CRPGDYGSDV SHLNLHKTFC IPHGGGGPGM
GPIGVKAHLA PFLPSHPVVP MQSVNTSSSL GTISAAPWGS SAILPISWAY IKMMGSKGLV
HATEVAILNA NYMAKRLEGH YKILFKGRKG FVAHEFILDV RPFKKTANIE AVDVAKRLQD
YGFHAPTMSW PVAGTLMIEP TESEDKAEMD RFCDALMGIR QEIADIEEGR MDSRINPLKM
APHSLACISS SNWDRPYSRE YAAFPLPFIR PETKFWPTIS RIDDIYGDQH LVCTCPPMEV
YESPYEEKRA SS
//
