ID V5GZN1_IXORI Unreviewed; 998 AA.
AC V5GZN1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
OS Ixodes ricinus (Common tick) (Acarus ricinus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=34613 {ECO:0000313|EMBL:JAB76130.1};
RN [1] {ECO:0000313|EMBL:JAB76130.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland and midgut {ECO:0000313|EMBL:JAB76130.1};
RX PubMed=25765539;
RA Kotsyfakis M., Schwarz A., Erhart J., Ribeiro J.M.;
RT "Tissue- and time-dependent transcription in Ixodes ricinus salivary glands
RT and midguts when blood feeding on the vertebrate host.";
RL Sci. Rep. 5:9103-9103(2015).
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; GANP01008338; JAB76130.1; -; mRNA.
DR AlphaFoldDB; V5GZN1; -.
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 2: Evidence at transcript level;
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 Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 49..471
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 570..713
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT DOMAIN 816..937
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 738
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 998 AA; 110408 MW; 888B992A04B18E1A CRC64;
MQRIPRLGAL MRGDVKQILE RASVILKRSV RPASTLDRLL PVHDDFCSRH LGPREKDQKA
MLEYMGLKNI AELIDRTVPS SIRLNREMKL DQPLREEELM ERAQTIANMN QVWRSYIGMG
YYNCLTPPTI MRNVFENPGW TTQYTPYQAE IAQGRLESLL NYQTMVTDLT GLDVANASLL
DEGTAAAEAM GLCSRHTKRK RFYVSDKVHP QTLAVVQTRA DALGIEVVVS DCASMDFSKK
DFCGALFQYP DTEGSVRDFS ELVQACHDAK ALAVCATDLL ALTVLKPPGE FGADIAVGTS
QRLGIPLNYG GPHAAFFATR NSLMRLMPGR VVGVTRDAEG GKAYRLALQT REQHIRRDKA
TSNICTAQAL LANMSALYAV YHGPDGVRDI ATRVHHSTLI LATGVAKGGH GVIHPDFFDT
LKVSPASSLQ AIRDRATEKR INLRYFEDGT VGVSLDETVT EKDLDDLLWV FDCKQKSAEL
AEELGDQPNR SILQSKHKRT SSFLQHAVFN TYHSETQIVR YMKQLENKDV SLVHSMIPLG
SCTMKLNSTT EMMPSSLPNF ANLHPFVPPD QARGYARLFE ELEQDLCEIT GYDRVCLQPN
SGAQGEYAGL RAISSYFDAR GEKQRKVCLI PMSAHGTNPA SAHMAGMAVD PINMAKDGSI
DVAHLKAKLD QHADKVACIM ITYPSTNGIY EETIRDVCEL VHGAGAQVYL DGANMNAQVG
ICRPGDYGSD VSHLNLHKTF CIPHGGGGPG MGPIGVKAHL APFLPSHPIA DPSMARGGDP
RHSFGAVCAA PWGSSAILPI SWAYIKMMGS RGLRRATEVA MLNANYMRKR LDAHYKVLYL
GQNGFVAHEF ILDMRDFKKT TGVEAMDVAK RLQDYGFHAP TVSFPVSGCL MVEPTESEDK
QELDRFCDAL ILIRDEIRAI EEGRMDAKVN PLKMSPHPQK VVCSNDWDRP YSREQAAFPA
KFVTPESKVW PTVGRIDDIY GDTNLMCSCP PMDSYEPL
//
