ID   GCSP_NOSP7              Reviewed;         979 AA.
AC   B2J427;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=Npun_R3754;
OS   Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=63737;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29133 / PCC 73102;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA   Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT   "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL   Submitted (APR-2008) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001037; ACC82139.1; -; Genomic_DNA.
DR   RefSeq; WP_012410110.1; NC_010628.1.
DR   AlphaFoldDB; B2J427; -.
DR   SMR; B2J427; -.
DR   STRING; 63737.Npun_R3754; -.
DR   EnsemblBacteria; ACC82139; ACC82139; Npun_R3754.
DR   KEGG; npu:Npun_R3754; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_3; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   PhylomeDB; B2J427; -.
DR   Proteomes; UP000001191; 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; Reference proteome.
FT   CHAIN           1..979
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000132445"
FT   MOD_RES         724
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   979 AA;  106853 MW;  7D692D6F2AE0E4E9 CRC64;
     MVLNAPILKS NEQQVLNQKS QKLSSFAPRH IGPNSDDIQQ MLKVLGFPSL DALIDKTVPQ
     TIRLKQPLKL PEAESEYAAL ASLKKIAAKN QVFRSYIGMG YYDTITPLVI GRNILENPGW
     YTAYTPYQPE IAQGRLEALL NFQTLIIDLT GLEIANASLL DEATAAAEAM SLSYGVSKNQ
     ANAYFVSHDC HPQTIDVLQT RAKPLGINII VGDHQTFDFD RAIFGAVLQY PASDGTIYDY
     RAFIEKAHAK GALVTVAADP LSLTLLTPPG EFGADIAVGS TQRFGIPLGF GGPHAAYFAT
     KEEYKRLVPG RIVGVSKDAQ GKPALRLALQ TREQHIRREK ATSNICTAQV LLAVMASMYA
     VYHGPDGLKQ IAENIHQLTL MLAAGLKHLG YKISSEHFFD TLRVELGTRS LEVILEACQA
     RNINLRIFDD TAVGISVDET TTADDLIELF EIFAAPDSLL FGFKEIGDLI AARRKSSLQN
     STFARTSNYL THPVFNRYHS ETELLRYLHK LESKDLSLTT SMIPLGSCTM KLNATAEMIP
     VTWEEFGKIH PFAPASQTQG YQILFQQLEA WLAEITGFAG ISLQPNAGSQ GEYAGLLVIR
     QYHENRGEAH RNVCLIPTSA HGTNPASAVM CGMKVVAVAC DSQGNIDVDD LKAKAEKHSH
     ELAALMVTYP STHGVFEEPI QEICAVVHSH GGQVYMDGAN MNAQVGICRP GDIGADVCHL
     NLHKTFCIPH GGGGPGMGPI GVASHLVPFL PGHPVVTIND STQHSHIGAV AAAPWGSASI
     LVISWMYIAM MGADGLTQAT KVAILNANYI AKKLESYYPV LYQGKNGLVA HECILDLRSL
     KKSAAIEIDD VAKRLMDYGF HAPTVSWPVG GTIMVEPTES ESKQELDRFC DALIAIRQEI
     AEIEVGKVDA QDNVLKNAPH TAESLITGEW QHPYSREQAA YPAPWTREYK FWPAVGRIDA
     AFGDRNFVCS CLPMDAYSS