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   27-MAR-2024, entry version 110.
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};
GN   OrderedLocusNames=PD_0620;
OS   Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC   Bacteria; Pseudomonadota; 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=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; 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   KEGG; xft:PD_0620; -.
DR   HOGENOM; CLU_004620_2_1_6; -.
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; 3.90.1150.10; 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   Oxidoreductase; Pyridoxal phosphate; Reference proteome.
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
//