ID   GCSP_CERS5              Reviewed;         956 AA.
AC   A4WUX2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=Rsph17025_2297;
OS   Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=349102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17025 / ATH 2.4.3;
RG   US DOE Joint Genome Institute;
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   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M.,
RA   Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025.";
RL   Submitted (APR-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=(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; CP000661; ABP71186.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4WUX2; -.
DR   SMR; A4WUX2; -.
DR   STRING; 349102.Rsph17025_2297; -.
DR   EnsemblBacteria; ABP71186; ABP71186; Rsph17025_2297.
DR   KEGG; rsq:Rsph17025_2297; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_4_1_5; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   BioCyc; RSPH349102:G1G8M-2369-MON; -.
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..956
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045603"
FT   MOD_RES         697
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   956 AA;  103186 MW;  AE93CC7DEC3410D3 CRC64;
     MTFTPTDYNA YDFANRRHIG PSPSEMEEML RVVGVSSLDQ LIEETVPASI RQDQPLDWAP
     LAEHELLQKM REVAAKNRVM VSLIGQGYYG TVTPPAIQRN ILENPAWYTA YTPYQPEIAQ
     GRLEALLNYQ TMVADLTGLP VANASLLDEA TAAAEAMTMA ERASKSKARA FFVDADCHPQ
     TIAVIRTRAE PLGIEVIVGH PAQLVPEDVF GALFQYPGTY GLVRDFTREI AALHEAKALA
     IVATDLLALC LLKEPGAMGA DIAIGSSQRF GVPMGYGGPH AAFMSCRDEL KRSMPGRLVG
     VSVDARGNKA YRLALQTREQ HIRREKATSN VCTAQALLAV MASFYAVFHG PKGLRHIAER
     VHLNTVRLAQ ALKEAGARVS PEAFFDTITV EVGVGQAGIL AAARHRGINL RKVGRDRVGI
     SLDETTDAGV IARVLDAFGI HDPAPASVGL GFPEAMLRES AYLSHPVFDM NRAESEMMRY
     MRRLSDRDLA LDRAMIPLGS CTMKLNAAAE MMPITWPEFA TLHPFAPPEQ AAGYTEAIRD
     LSDRLCRITG YDAMSMQPNS GAQGEYAGLL TILAYHRARG EGQRTICLIP MSAHGTNPAS
     AQMAGMKVVV VKSAPNGDVD LDDFRDKAAA AGDRLAACMI TYPSTHGVFE ETVRDVCRIT
     HEHGGQVYID GANMNAMVGL VQPGAIGGDV SHLNLHKTFA IPHGGGGPGM GPIGVKAHLA
     PYLPGHPETG GPLAGGQIVA THEGPVSAAP YGSASILLIS WAYCLMMGGE GLTQATRVAI
     LNANYVAARL RGAYDVLFMG NRGRVAHECI LDTRPFAEAG VTVDDIAKRL IDNGFHAPTM
     SWPVPGTLMV EPTESETKAE IDRFITALLA IREEIRAVEA GEIAAADSPL RHAPHTVEDL
     VADWDRNYPR EQGCFPPGAF RVDKYWPPVG RVDNAWGDRN LVCICPPVES YSIAAQ