ID GCSP_NEIG2 Reviewed; 950 AA.
AC B4RN40;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
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=NGK_1550;
OS Neisseria gonorrhoeae (strain NCCP11945).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=521006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCCP11945;
RX PubMed=18586945; DOI=10.1128/jb.00566-08;
RA Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.;
RT "Complete genome sequence of Neisseria gonorrhoeae NCCP11945.";
RL J. Bacteriol. 190:6035-6036(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=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; CP001050; ACF30206.1; -; Genomic_DNA.
DR RefSeq; WP_012503780.1; NC_011035.1.
DR AlphaFoldDB; B4RN40; -.
DR SMR; B4RN40; -.
DR KEGG; ngk:NGK_1550; -.
DR HOGENOM; CLU_004620_3_2_4; -.
DR Proteomes; UP000002564; 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.
FT CHAIN 1..950
FT /note="Glycine dehydrogenase (decarboxylating)"
FT /id="PRO_1000132444"
FT MOD_RES 698
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ SEQUENCE 950 AA; 104165 MW; B999CDC250A03C43 CRC64;
MKLSELFNPN EFAARHLSFG DEAALLAAVG EKSMDDFVGN 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 AQALLTNLAG MYAVYHGPKG VKRIANRIHT
LASVFADALV SDGLKVVHEV FFDTVTVDFG SKEKADQVFA AALESGYNLR RVNNTQVAAA
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
//
