ID A0A067RMZ2_ZOONE Unreviewed; 1018 AA.
AC A0A067RMZ2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=L798_03687 {ECO:0000313|EMBL:KDR21089.1};
OS Zootermopsis nevadensis (Dampwood termite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Termopsidae; Zootermopsis.
OX NCBI_TaxID=136037 {ECO:0000313|EMBL:KDR21089.1, ECO:0000313|Proteomes:UP000027135};
RN [1] {ECO:0000313|EMBL:KDR21089.1, ECO:0000313|Proteomes:UP000027135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole organism {ECO:0000313|EMBL:KDR21089.1};
RX PubMed=24845553; DOI=10.1038/ncomms4636;
RA Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z.,
RA Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W.,
RA Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M.,
RA Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T.,
RA Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., Zhou J.,
RA Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., Liberles D.A., Roe R.M.,
RA Vargo E.L., Vilcinskas A., Wang J., Bornberg-Bauer E., Korb J., Zhang G.,
RA Liebig J.;
RT "Molecular traces of alternative social organization in a termite genome.";
RL Nat. Commun. 5:3636-3636(2014).
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; KK852572; KDR21089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067RMZ2; -.
DR STRING; 136037.A0A067RMZ2; -.
DR EnsemblMetazoa; KDR21089; KDR21089; L798_03687.
DR eggNOG; KOG2040; Eukaryota.
DR InParanoid; A0A067RMZ2; -.
DR OMA; RNLICTC; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000027135; 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; 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:UP000027135};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 72..494
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 837..959
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 760
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1018 AA; 113592 MW; B914E2432D458F66 CRC64;
MYRITAATTL RNKKLRELFK KRLVEPTVYC VFTTNPNPLP NDVSNITVNK LDNDGLQRLA
KLFPKREEFP ARHIGPRDHE QTQMLELLGF RTLDEMTDMA VPAKIRLNKD LEIEEPVGEY
ELIKRIREIA EKNKIWRSYI GMGYNNCCVP HTIMRNIFEN PGWTTQYTPY QPEVAQGRLE
GLLNYQTMVT DLTGMEVANA SLLDEGTAAA EAMSLCHRHT KRRRLFLSDQ LHPQTVSVVQ
TRADSLGLTV ELGNVFAADF SNRDIAGVLF QYPDTGGSVH DYSEVVQRAH SNGTLVCCAT
DLLALTLLRP PSEFDVDISL GTSQRFGVPL GYGGPHAGFF ACRQSLVRLM PGRMIGVTRD
ASGRDAYRLA LQTREQHIRR DKATSNICTA QALLANMSAM YAVYHGPHGL REIATRIHKS
ALLLSEGVKE GGNTVTNHIF FDTIRINPAM DQGEIQHRAR QKQINLRFYP DETVGVSLDE
TVTIQDIEDL LWVFGSRLSA EEVAGSCDMN EGSIFQSSFR RTSPYLTHPV FNSYHSETRI
VRYMKTLENK DVSLVHSMIP LGSCTMKLNS TTEMMPCSFQ HFTDIHPFAP LDQSLGYQQL
FEELQQDLCA ITGYDRISFQ PNSGAQGEYA GLSAIKCYHE ARSEGHRNIC LIPVSAHGTN
PASAQMAGMK VEPINVCRDG SIDISHLASK VEKHGKNLAC LMITYPSTNG VFEETIADVC
HMIHDNGGQV YLDGANMNAQ VGLCRPGDYG SDVSHLNLHK TFCIPHGGGG PGMGPIGVKA
HLAPFLPTHP VVNPMADMGR HSKSFGVVSA APFGSSAILP ISWAYIKMMG PRGLRKATQV
AILNANYMSK RLEGHYKTLF KGQKSSLVAH EFILDVRDFK KTANIEAVDI AKRLMDYGFH
APTMSWPVSG TLMIEPTESE DKQELDRFCD ALIYIRQEIN EIEEGRMDIR TNPLTMAPHT
QARVISNDWN RPYTREQAAF PAPFVHPETK VWPSVGRIDD IYGDKHLVCT CPPILPAY
//
