GCSP_XYLFT
ID GCSP_XYLFT Reviewed; 993 AA.
AC Q87DR1;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Glycine dehydrogenase (decarboxylating) {ECO:0000255|HAMAP-Rule:MF_00711};
DE EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine cleavage system P-protein {ECO:0000255|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine decarboxylase {ECO:0000255|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000255|HAMAP-Rule:MF_00711};
GN Name=gcvP {ECO:0000255|HAMAP-Rule:MF_00711}; OrderedLocusNames=PD_0620;
OS Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=183190;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Temecula1 / ATCC 700964;
RX PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT "Comparative analyses of the complete genome sequences of Pierce's disease
RT and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL J. Bacteriol. 185:1018-1026(2003).
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. The P protein binds the alpha-amino group of glycine through
CC its pyridoxal phosphate cofactor; CO(2) is released and the remaining
CC methylamine moiety is then transferred to the lipoamide cofactor of the
CC H protein. {ECO:0000255|HAMAP-Rule:MF_00711}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] +
CC glycine + H(+) = (R)-N(6)-(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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00711};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00711};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000255|HAMAP-Rule:MF_00711}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000255|HAMAP-
CC Rule:MF_00711}.
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DR EMBL; AE009442; AAO28492.1; -; Genomic_DNA.
DR AlphaFoldDB; Q87DR1; -.
DR SMR; Q87DR1; -.
DR EnsemblBacteria; AAO28492; AAO28492; PD_0620.
DR KEGG; xft:PD_0620; -.
DR HOGENOM; CLU_004620_2_1_6; -.
DR OMA; CVPMSEY; -.
DR Proteomes; UP000002516; Chromosome.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR CDD; cd00613; GDC-P; 2.
DR Gene3D; 3.40.640.10; -; 2.
DR Gene3D; 3.90.1150.10; -; 2.
DR HAMAP; MF_00711; GcvP; 1.
DR InterPro; IPR003437; GcvP.
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 PANTHER; PTHR11773; PTHR11773; 1.
DR Pfam; PF02347; GDC-P; 2.
DR SUPFAM; SSF53383; SSF53383; 2.
DR TIGRFAMs; TIGR00461; gcvP; 1.
PE 3: Inferred from homology;
KW Oxidoreductase; Pyridoxal phosphate.
FT CHAIN 1..993
FT /note="Glycine dehydrogenase (decarboxylating)"
FT /id="PRO_0000166951"
FT MOD_RES 715
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ SEQUENCE 993 AA; 107647 MW; BCC04E829C442F43 CRC64;
MFSASHFCSG SLMMSHPLSS LRDLEYHGAF VERHIGPNDV EIAQMLRVVG YDSLESLTDA
IVPEKIRSTV ALDLPKGITE EEALAKIRVI ANKNRVFRSF IGQGYYGTHT PKVILRNILE
NPAWYTAYTP YQAEISQGRM EALINFQTMC ADLTGMEIAN ASLLDEATAA AEAMSLAKRS
AKSRSDLFFV HDAVHPQTLE LLRTRAEPLG IVLRVGTPEE ALQVDVFGIL LQYPDTFGRI
GDHRVLADAV HARGGLVAVA SDLLALTLIT PPGEWGADIV VGNSQRFGVP FGFGGPHAGF
MACRDIYKRS IPGRLIGVSV DAAGHPAYRL ALQTREQHIR REKATSNICT AQVLLAVMAS
MYAVYHGPQG LLRIAWRTHR MAAILAAALR GAGLTVGEYF FDTLHIVGID ALAIHCAAAA
AGMNLRMIDN AQIGISLDET VTRSDVVALG QVFGVQVDVE ALDAITADAL PAGLLRSSAF
LTHPVFNTHH SEHELLRYLR MLADKDLAMD RTMIPLGSCT MKLNATAEMI PVTWQEFACI
HPLAPVVQWS GYRQLIDELE AMLVECTGYD AISLQPNSGA QGEYAGLLAI RAYHRSRGEE
RRNVCLIPES AHGTNPASAQ LCGMQVVIIK CDRSGNVDVD DLRMKAEKYS DTLAALMVTY
PSTHGVFEEA ITEICEIVHA HGGQVYTDGA NMNALVGVAK PGRWGSDVSH LNLHKTFCIP
HGGGGPGVGP CAVKAHLAPF LPKTLPLPGD AAGLPVQGTQ EAKVGMVSAA NFGSASILPV
SWMYITMMGA AGLRKATQVA LLNANYIAKR LAPHYKTLYT GRHGLVAHEC ILDVRSLEKV
SGVSAEDIAK RLIDFGFHAP TLSFPVAGTL MVEPTESESQ QELDRFVDAM IQIRGEIAAI
EKGHLDPEDN PLKQAPHTAV QVMASQWGHA YSRELAAFPL GVLHHAKYWP PVARVDNVYG
DKHVMCACIP VEAYKEKGDS EIQDLIEEDA SRC
