ID E6MXB0_NEIMH Unreviewed; 950 AA.
AC E6MXB0;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Glycine dehydrogenase (decarboxylating) {ECO:0000256|HAMAP-Rule:MF_00711};
DE EC=1.4.4.2 {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine cleavage system P-protein {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine decarboxylase {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|HAMAP-Rule:MF_00711};
GN Name=gcvP {ECO:0000256|HAMAP-Rule:MF_00711,
GN ECO:0000313|EMBL:EFV63780.1};
GN ORFNames=NMH_1313 {ECO:0000313|EMBL:EFV63780.1};
OS Neisseria meningitidis serogroup B / serotype 15 (strain H44/76).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=909420 {ECO:0000313|EMBL:EFV63780.1, ECO:0000313|Proteomes:UP000032707};
RN [1] {ECO:0000313|EMBL:EFV63780.1, ECO:0000313|Proteomes:UP000032707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H44/76 {ECO:0000313|EMBL:EFV63780.1,
RC ECO:0000313|Proteomes:UP000032707};
RX PubMed=21378179; DOI=10.1128/JB.01331-10;
RA Piet J.R., Huis In 't Veld R.A., van Schaik B.D., van Kampen A.H., Baas F.,
RA van de Beek D., Pannekoek Y., van der Ende A.;
RT "Genome sequence of Neisseria meningitidis serogroup B strain H44/76.";
RL J. Bacteriol. 193:2371-2372(2011).
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:0000256|ARBA:ARBA00003788, ECO:0000256|HAMAP-
CC 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;
CC Evidence={ECO:0000256|ARBA:ARBA00043839, ECO:0000256|HAMAP-
CC Rule:MF_00711};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00711, ECO:0000256|PIRSR:PIRSR603437-50};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|ARBA:ARBA00011690, ECO:0000256|HAMAP-
CC Rule:MF_00711}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000256|ARBA:ARBA00010756,
CC ECO:0000256|HAMAP-Rule:MF_00711}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFV63780.1}.
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DR EMBL; AEQZ01000021; EFV63780.1; -; Genomic_DNA.
DR RefSeq; WP_002244257.1; NZ_AEQZ01000021.1.
DR AlphaFoldDB; E6MXB0; -.
DR PATRIC; fig|909420.3.peg.726; -.
DR Proteomes; UP000032707; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00711};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00711,
KW ECO:0000256|PIRSR:PIRSR603437-50}.
FT DOMAIN 21..437
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 471..729
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 771..892
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 698
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 950 AA; 103848 MW; 6BB67785F0C68212 CRC64;
MKLSELFNPN EFAARHLSFG DEAALLAAVG EKSMDDFVGN TVPQSIRMPS ELDLPDALTE
ADALAKLKGI ASKNVINKSY IGLGYYPTRV PNVILRNVLE NPGWYTAYTP YQAEIAQGRL
EALLNFQQVC IDLTGFPVAG ASLLDEATAA AEAMAMAHRV GKVKSGRFFV DERVYPQTLD
VMKTRAKYFG FELVVGDFVK ADEGEYFGAL FQYVGKDGDV QDLQDVISRL KAKGTIVVVA
TDIMSLVLLK SPAELGADIA LGNTQRFGVP MGFGGPHAAY FAFKDAFKRS APGRIIGVSK
DASGKPALRM ALSTREQHIR REKATSNICT AQALLANLAG MYAVYHGPEG VKRIANRIHA
LASAFADALV SDGIKVVHEV FFDTVTVDFG NKEKADQVFA AALESGYNLR RVNDTQVAAA
FHETSAYEDL VDLYRAFTGK DAFAFADDVK GRLNAELLRQ DDILQHPVFN RYHTEHEMLR
YLKKLEDRDL AMNRSMISLG SCTMKLNATA EMLPITWAEF SDIHPYAPEA QTAGYRELLA
DMENSLKSIT GFDAISFQPN SGAQGEYSGM LAIRRYQEAQ GEAHRNICLI PKSAHGTNPA
TAAMLGLKVV VVDTDEHGNV NIDDLKAKAE QYRDALSAIM ITYPSTHGVY EEGIRDICRI
IHENGGQVYM DGANLNAQIG IMQPAEVGAD VLHMNLHKTF CIPHGGGGPG MGPIGLKAHL
APFAPGHALT DTHSTSAGQT AVAAAAYGSA SILPITWMYL TMMGKQGMEQ ATRWALLNAN
YVAKALGEDY PILYTGKNGR VAHECIVDLR PLKAESGITE TDIAKRLMDY GFHAPTVSFP
VAGTLMIEPT ESESKAELDR FIAALKQIKQ EVLKVGRGEW PKDDNPLVNA PHTAADITGN
WAHPYSREEA VFPLPFVREH KFWPSVNRVD DVYGDRNLVC SCPPMENYED
//
