ID   GCSP_XANOM              Reviewed;         984 AA.
AC   Q2P021;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 102.
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=XOO3351;
OS   Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=342109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 311018;
RA   Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT   "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT   large numbers of effector genes and insertion sequences to its race
RT   diversity.";
RL   Jpn. Agric. Res. Q. 39:275-287(2005).
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; AP008229; BAE70106.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2P021; -.
DR   SMR; Q2P021; -.
DR   KEGG; xom:XOO3351; -.
DR   HOGENOM; CLU_004620_3_2_6; -.
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; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate.
FT   CHAIN           1..984
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045628"
FT   MOD_RES         702
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   984 AA;  105426 MW;  A6D61E47C931048F CRC64;
     MSQTPSSLCD LEHHSAFVER HIGPNDAEIA QMLEVVGHAS LDALTDAIVP GNIKSPAPLA
     LPEAITEEEA LVKIRAIADK NTVYRNFIGQ GYYGTHTPKV ILRNILENPA WYTAYTPYQA
     EISQGRMEAL INFQTLCADL TGMQIANASL LDEATAAAEA MTLAKRSAKS RSDIFFVHDA
     VHPQTLELLR TRAEPLDIML RVGTPEEALQ AECFGVLLQY PDSFGHIGDH AALADAVHAQ
     GGLVAVATDL LALTLIAAPG QWGADIVVGN SQRFGVPFGF GGPHAAFMAC RDAYKRSMPG
     RLIGVSIDAA GNPAYRLTLQ TREQHIRREK ATSNICTAQV LLAVMASMYA VYHGPDGLTR
     IARRTHRLAA ILAAALRGAG VTVGEHFFDT LHVKAIDADA IHARARAAGI NLRAIDSEAV
     GISLDETTTR ADVVALAQLF GAMADVDALD AATADALPQG LLRSSAFLTH PVFNTHHSEH
     ELLRYMRSLA DKDLAMDRTM IPLGSCTMKL NATAEMIPVT WPEFGAIHPL APAEQSAGYA
     QLIDELEAML VECTGYDAVS LQPNSGAQGE YAGLLAIRAY HRSRGEAHRD ICLIPESAHG
     TNPASAQMCG MTVVVTKCDA NGNVDVDDIR AKAEKYSDRL AALMITYPST HGVFEEDVVA
     ICEAVHAHGG QVYTDGANMN ALVGVAKPGK WGSDVSHLNL HKTFCIPHGG GGPGVGPCAV
     KSHLAPFLPR AGLHAGEGQT AAIHGGGFNS GSGSGHSSRI GGMVSAAAYG SASILPISWM
     YVTMMGSAGL RKATQVALLN ANYIAKRLAP HYKTLYTGRN GLVAHECILD VRPLEKTSGI
     GAEDIAKRLI DFGFHAPTLS FPVAGTLMVE PTESESQHEL DRFIDAMIQI REEIRAIEDG
     RLDREDNPLK HAPHTATQVS ASEWTHAYPR ELAAFPLPSL KQQKYWPPVA RVDNVYGDKN
     VMCACIPVDA YKIPVDAYKE DAEA
//