ID   GCSP_NEIM0              Reviewed;         950 AA.
AC   A9M1P7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=NMCC_1587;
OS   Neisseria meningitidis serogroup C (strain 053442).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=374833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=053442;
RX   PubMed=18031983; DOI=10.1016/j.ygeno.2007.10.004;
RA   Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., Xiong Z.,
RA   Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., Shao Z.,
RA   Liang X., Xu J., Jin Q.;
RT   "Characterization of ST-4821 complex, a unique Neisseria meningitidis
RT   clone.";
RL   Genomics 91:78-87(2008).
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; CP000381; ABX73736.1; -; Genomic_DNA.
DR   RefSeq; WP_002258673.1; NC_010120.1.
DR   AlphaFoldDB; A9M1P7; -.
DR   SMR; A9M1P7; -.
DR   PRIDE; A9M1P7; -.
DR   EnsemblBacteria; ABX73736; ABX73736; NMCC_1587.
DR   KEGG; nmn:NMCC_1587; -.
DR   HOGENOM; CLU_004620_3_2_4; -.
DR   OMA; CVPMSEY; -.
DR   Proteomes; UP000001177; 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   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..950
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000083210"
FT   MOD_RES         698
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   950 AA;  103931 MW;  7D95ED0037B62BC6 CRC64;
     MKLSELFNPD EFAARHLSFG DEAALLAAVG EKSMDDFVGN TVPQSIRMPS ELDLPEALTE
     ADALAKLKGI ASKNMINKSY IGLGYYPTRV PNVILRNVLE NPGWYTAYTP YQAEIAQGRL
     EALLNFQQVC IDLTGFPVAG ASLLDEATAA AEAMAMAHRV GKVKSERFFV DARVYPQTLD
     VMKTRAKYFG FELVVGDFAQ ADEGEYFGAL FQYVGKDGDV QDLQDVIGRL KAKGTIVAVS
     ADIMSLVLLK SPAELGADIA LGNTQRFGVP MGFGGPHAAY FAFKDEFKRS APGRIIGVSK
     DASGKPALRM ALSTREQHIR REKATSNICT AQALLANLAG MYAVYHGPEG VKRIANRIHA
     LASAFADALV SDGINVVHKV FFDTVTVDFG NKEKADQVFA AALESGYNLR RVNDTQVAAA
     FHETSACEDL VDLYRAFTGK DTFAFADDVK GRLNAELLRQ DDILQHPVFN RYHTEHEMLR
     YLKKLEDRDL AMNRSMISLG SCTMKLNATA EMLPITWAEF SDIHPYAPEA QTAGYRELLA
     DMENSLKSIT GFDAISFQPN SGAQGEYSGM LAIRRYQEAQ GEAQRNICLI PKSAHGTNPA
     TAAMLGLKVV VVDTDEHGNV NIDDLKAKAE QHRDALSAIM ITYPSTHGVY EEGIRDICRI
     VHENGGQVYM DGANLNAQIG IMQPAEVGAD VLHMNLHKTF CIPHGGGGPG MGPIGLKAHL
     APFAPGHALT DTHSASADQT AVAAAAFGSA SILPITWMYL TMMGKQGMEQ ATRWALLNAN
     YVAKRLSEDY PILYTGKNGR VAHECIVDLR PLKAESGITE TDIAKRLMDY GFHAPTVSFP
     VAGTLMIEPT ESESKAELDR FIAALKQIKQ EVLKVGRGEW PKEDNPLVNA PHTASDVTGE
     WAHPYSREEA VFPLPFVREH KFWPSVNRVD DVYGDRNLVC SCPPMENYED