ID GCSP_NEIG1 Reviewed; 950 AA. AC Q5F761; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 27-MAR-2024, entry version 104. 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=NGO1325; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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}. 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; AE004969; AAW89976.1; -; Genomic_DNA. DR RefSeq; WP_003705868.1; NC_002946.2. DR RefSeq; YP_208388.1; NC_002946.2. DR AlphaFoldDB; Q5F761; -. DR SMR; Q5F761; -. DR STRING; 242231.NGO_1325; -. DR KEGG; ngo:NGO_1325; -. DR PATRIC; fig|242231.10.peg.1559; -. DR HOGENOM; CLU_004620_3_2_4; -. DR Proteomes; UP000000535; 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; 3.90.1150.10; 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:SF13; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 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; Reference proteome. FT CHAIN 1..950 FT /note="Glycine dehydrogenase (decarboxylating)" FT /id="PRO_0000227108" FT MOD_RES 698 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00711" SQ SEQUENCE 950 AA; 104080 MW; FFD4BDE3B5A7437E CRC64; MKLSELFNPN EFAARHLSFG DEAALLAAVG EKSMDEFVGN TLPQSIRMPS ELDLPEALTE ADALAKLKGI ASKNVINKSY IGLGYYPTRV PNVILRNVLE NPGWYTAYTP YQAEIAQGRL EALLNFQQVC IDLTGFPVAG ASLLDEATAA AEAMAMAHRV GKVKSERFFV DARVYPQTLD VMKTRAKYFG FELVVSDFAQ ADEGEYFGAL FQYVGKDGDV QDLQDVIGRL KAKGTIVAVA ADIMSLVLLK SPAELGADIA LGNTQRFGVP MGFGGPHAAY FAFKDEFKRS APGRIIGVSK DASGKPALRM ALSTREQHIR REKATSNICT AQALLANLAG MYAVYHGPKG VKRIANRIHT LASVFADALV SDGLKVVHEV FFDTVTVDFG SKEKADQVFA AALESGYNLR SVNNTQVAAA FHETSVYEDL ADLYRAFTGK DTFTFADDVK GRLNAELLRQ DDILQHPVYN SYHTEHEMLR YLKKLEDRDL AMNRSMISLG SCTMKLNATA EMLPITWTEF SDIHPYAPEA QTAGYRELLA DMENSLKAIT GFDAISFQPN SGAQGEYSGM LAIRRYQEAQ GEAHRNICLI PKSAHGTNPA TAAMLGLKVV VVDTDEHGNV NIDDLKAKAE QHRDALSAIM ITYPSTHGVY EEGIRDICRI IHENGGQVYM DGANLNAQIG IMQPAEVGAD VLHMNLHKTF CIPHGGGGPG MGPIGLKAHL APFAPGHTLT DTHSASAGQT SVAAAAFGSA SILPITWMYL TMMGKQGMEQ ATRWALLNAN YVAKRLSEDY PILYTGKNGR IAHECIVDLR PLKAESGITE TDIAKRLMDY GFHAPTVSFP VAGTLMIEPT ESESKAELDR FIAALKSIRR EVQKVIDGEW PKDDNPLVNA PHTAADITGE WAHPYSREEA VFPLPFVREH KFWPFVNRVD DVYGDRNLVC SCPPMENYED //