ID   GCSP_CERS1              Reviewed;         956 AA.
AC   A3PI15;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 91.
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=Rsph17029_0870;
OS   Cereibacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cereibacter.
OX   NCBI_TaxID=349101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17029 / ATH 2.4.9;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.,
RA   Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides ATCC 17029.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000577; ABN75981.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3PI15; -.
DR   SMR; A3PI15; -.
DR   KEGG; rsh:Rsph17029_0870; -.
DR   HOGENOM; CLU_004620_3_2_5; -.
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..956
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045602"
FT   MOD_RES         697
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   956 AA;  103072 MW;  4671F169C036BEF0 CRC64;
     MSFTPTDYNA YDFANRRHIG PSPSEMEEML RVVGVSSLDQ LIEETVPASI RQETPLDWAP
     LAEHELLARM REVAGKNRVM TSLIGQGYYG TVTPPAIQRN ILENPAWYTA YTPYQPEIAQ
     GRLEALLNYQ TMVADLTGLP VANASLLDEA TAAAEAMTMA ERASKSKARA FFVDADCHPQ
     TISVIRTRAE PLGIEVIVGH PAQLVPEDVF GALFQYPGTY GLVRDFTRDI AALHEAKALA
     VVATDLLALC LLKEPGAMGA DIAIGSSQRF GVPMGYGGPH AAFMSCKDDL KRSMPGRLVG
     VSVDARGNKA YRLALQTREQ HIRREKATSN VCTAQALLAV MASFYAVFHG PRGLRAIAER
     VHLNTVRLAT ALKEAGARVS PEAFFDTITV EVGVGQAGIL AAARHRGINL RKVGRDRVGI
     SLDETTDAGV IARVLDAFGI HEPAPAKVGL GFPEPLLRET GYLSHPVFQM NRAESEMMRY
     MRRLSDRDLA LDRAMIPLGS CTMKLNAAAE MMPITWPEFG TLHPFAPADQ AAGYHEAIGD
     LAQRLCRITG YDAMSMQPNS GAQGEYAGLL TILAYHRARG EAERTICLIP VSAHGTNPAS
     AQMAGMKVVV VKSAPNGDVD LEDFRDKAAA AGDRLAACMI TYPSTHGVFE ETVREVCRIT
     HEHGGQVYID GANMNAMVGL VQPGAIGGDV SHLNLHKTFA IPHGGGGPGM GPIGVKAHLA
     PYLPGHPEVT GPLTGGHDEA ADEGPVSAAP YGSASILLIS WAYCLMMGGE GLTQATRVAI
     LNANYIAARL RGAYKVLFMG NRGRVAHECI LDTRPFAEAG VTVDDIAKRL IDNGFHAPTM
     SWPVPGTLMV EPTESETKAE IDRFVAALLA IREEIRAVEE GEIAAGDSPL RHAPHTVEDL
     VADWDRKYPR EQGCFPPGSF RVDKYWPPVG RVDNAWGDRN LVCTCPPVES YSIAAQ
//