ID A0A671LF51_9TELE Unreviewed; 1025 AA.
AC A0A671LF51;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 26.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN Name=LOC107699756 {ECO:0000313|Ensembl:ENSSANP00000018946.1};
OS Sinocyclocheilus anshuiensis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Sinocyclocheilus.
OX NCBI_TaxID=1608454 {ECO:0000313|Ensembl:ENSSANP00000018946.1, ECO:0000313|Proteomes:UP000472260};
RN [1] {ECO:0000313|Ensembl:ENSSANP00000018946.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSSANP00000018946.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. {ECO:0000256|RuleBase:RU364056}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage complex H protein]
CC + glycine + H(+) = N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-L-lysyl-
CC [glycine-cleavage complex H protein] + CO2; 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:ARBA00049026,
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: Homodimer. The glycine cleavage system is composed of four
CC proteins: P, T, L and H. {ECO:0000256|ARBA:ARBA00046415}.
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 RefSeq; XP_016356594.1; XM_016501108.1.
DR AlphaFoldDB; A0A671LF51; -.
DR Ensembl; ENSSANT00000020220.1; ENSSANP00000018946.1; ENSSANG00000009342.1.
DR GeneID; 107699756; -.
DR KEGG; sanh:107699756; -.
DR OrthoDB; 6537869at2759; -.
DR Proteomes; UP000472260; Unassembled WGS sequence.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:TreeGrafter.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016594; F:glycine binding; IEA:TreeGrafter.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:TreeGrafter.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:TreeGrafter.
DR CDD; cd00613; GDC-P; 2.
DR FunFam; 3.90.1150.10:FF:000025; Glycine cleavage system P protein; 1.
DR FunFam; 3.90.1150.10:FF:000153; Glycine dehydrogenase (decarboxylating); 1.
DR FunFam; 3.40.640.10:FF:000005; Glycine dehydrogenase (decarboxylating), mitochondrial; 1.
DR FunFam; 3.40.640.10:FF:000007; glycine dehydrogenase (Decarboxylating), mitochondrial; 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 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 NCBIfam; NF003346; PRK04366.1; 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|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR603437-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000472260};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 72..495
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 593..736
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT DOMAIN 836..957
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 761
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1025 AA; 113673 MW; 83A713DC74730800 CRC64;
MQSCAKSWRV VISRSIDARA PYRNISNKGG VFKKLQGLNA DVSANVRCMG TSQILWSRKI
ERILPRHDDF SERHIGPGDK EKQEMLSTLG LESVAQLIEN TVPASIRLGR SLKMDDPVCE
NEILDSLQKI ASRNKMWRSY IGMGYYNCSV PPVIQRNLLE NSGWVTQYTP YQPEVSQGRL
ESLLNYQTMV CDITGMAVAN ASLLDEGTAA AEAMQLCNRQ NKRRMFYIDT RCHPQTIAVV
QTRANYIGVK TLLKLPHEMD FSGKDVSGVL FQYPDTEGRV EDFTALVDRA HKGGALACCA
TDLLALCVLR PPSEFGVDIA LGSSQRFGVP LCYGGPHAAF FAVKENLVRM MPGRMVGVTR
DAAGKEVYRL ALQTREQHIR RDKATSNICT AQALLANMAS MFALYHGPQG LRHIAERTHN
ATLILAEGLK RAGHKLQHEN FFDTLKISCG VAGKDILEKA MQREINLRVY SDGLLGVSLD
ETVTERDLDD LLWIFGCESS AELIAEKMSE RTKGLLASPF KRTSKFLTHP VFNSYHSETN
IVRYMKRLEN KDISLVHSMI PLGSCTMKLN SSSELMPITW REFANIHPFV PLDQAEGYQQ
LFRQLERDLC EITGYDKISF QPNSGAQGEY AGLAAIKAYL NSKGESHRTV CLIPKSAHGT
NPASAQMAGM KVQVVEVDKD GNIDVSHLKA MVDKHKANLA AIMITYPSTN GVFEENVSEV
CELIHQNGGQ VYLDGANMNA QVGLCRPGDY GSDVSHLNLH KTFCIPHGGG GPGMGPIGVK
QHLALFLPSH PVVNMQSSNA GSSLGTISAA PWGSSAILPI SWAYIKMMGS KGLVHATEVA
ILNANYMAKR LETHYKILFR GSKGFVAHEF ILDVRPFKKS ANIEAVDVAK RLQDYGFHAP
TMSWPVAGTL MIEPTESEDK AELDRFCDSL LAIRQEIADI EEGQMDSRVN PLKMAPHSLA
CITSTTWDRP YSREYAAFPV PFVRPETKFW PTISRIDDIY GDQHLVCTCP PMDVYESPYE
ERASS
//
