ID I4E481_NEIME Unreviewed; 950 AA.
AC I4E481;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
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:CCA44145.1};
GN ORFNames=NMALPHA522_0604 {ECO:0000313|EMBL:CCA44145.1};
OS Neisseria meningitidis alpha522.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=996307 {ECO:0000313|EMBL:CCA44145.1};
RN [1] {ECO:0000313|EMBL:CCA44145.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Alpha522 {ECO:0000313|EMBL:CCA44145.1};
RA Schoen C., Blom J.;
RT "Draft genome of Neisseria meningitidis strain alpha522.";
RL Submitted (MAR-2011) 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: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}.
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DR EMBL; FR845703; CCA44145.1; -; Genomic_DNA.
DR AlphaFoldDB; I4E481; -.
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..732
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; 104207 MW; 35036EF2EA49B48C CRC64;
MKLSELFNPN EFAARHLSFG DEAALLAAVG EKSMDDFVGN TVPQSIRMPS ELDLPEALTE
ADALAKLKGI ASKNVINKSY IGLGYYPTRV PNVILRNVLE NPGWYTAYTP YQAEIAQGRL
EALLNFQQVC IDLTGFPVAG ASLLDEATAA AEAMAMAHRV GKVKSERFFV DERVYPQTLD
VMKTRAKYFG FELVVGDFAK ADEGEYFGAL FQYVGKDGDV QDLQSVIGRL KAKGTIVAVS
ADIMSLVLLK SPAELGADIA LGNTQRFGVP MGFGGPHAAY FAFKDEFKRS 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 GEAQRNICLI PKSAHGTNPA
TAAMLGLKVV VVDTDEHGNV NIDDLKAKAE QHRDALSAIM ITYPSTHGVY EEGIRDICRI
VHENGGQVYM DGANLNAQIG IMQPAEVGAD VLHMNLHKTF CIPHGGGGPG MGPIGLKAHL
APFAPGHVVT DMHNASADQT AVAAAAFGSA SILPITWMYL TMMGKQGMEQ ATRWALLNAN
YVAKRLSEDY PILYTGKNGR VAHECIVDLR PLKAESGITE TDIAKRLMDY GFHAPTVSFP
VAGTLMIEPT ESESKAELDR FIAALKQIKQ EVLKVERGEW PKEDNPLVNA PHTASDVTGE
WTHPYSREEA VFPLPFVREH KFWPFVNRVD DVYGDRNLVC SCPPMENYED
//
