ID   GCSP_PHOLL              Reviewed;         958 AA.
AC   Q7N199;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=plu3596;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
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; BX571871; CAE15969.1; -; Genomic_DNA.
DR   RefSeq; WP_011147763.1; NC_005126.1.
DR   AlphaFoldDB; Q7N199; -.
DR   SMR; Q7N199; -.
DR   STRING; 243265.plu3596; -.
DR   PRIDE; Q7N199; -.
DR   EnsemblBacteria; CAE15969; CAE15969; plu3596.
DR   GeneID; 24169636; -.
DR   KEGG; plu:plu3596; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_6; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   BioCyc; PLUM243265:PLU_RS17835-MON; -.
DR   Proteomes; UP000002514; 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   CDD; cd00613; GDC-P; 2.
DR   Gene3D; 3.40.640.10; -; 2.
DR   Gene3D; 3.90.1150.10; -; 1.
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; Reference proteome.
FT   CHAIN           1..958
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000166922"
FT   MOD_RES         708
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   958 AA;  105143 MW;  2379AB181E054E0B CRC64;
     MTQTLSQLEN QGEFIRRHIG SSAEQQKEML ATVGASSLND LTQKIVPRDI ALPEPPDVGG
     GATEQQALAE LKAIASQNKR YQSYIGMGYA PAVLPPVILR NLLENPGWYT AYTPYQPEVS
     QGRLESLLNF QQVTIDLTGL DIASASLLDE ATAAAEAMAM AKRISKLKNA DRFFVADDIH
     PQTLDVVRTR AETFGFDVIV DKAEKVLELD GVFGVLLQQV GTTGEVHDYA DLIAQLKQRK
     IIVSVAADLM ALLLLTAPGK QGADMVFGSA QRFGVPMGYG GPHAAFFASR DEFKRSMPGR
     IIGVSRDAAG NTALRMAMQT REQHIRREKA NSNICTAQVL LANIAAMYAV YHGSKGLKRI
     AGRIHRLTDI LAVGLQKAGF TLRYKTWFDT LTVEVADKAA VLARAEKAEI NLRTDTYGAV
     GITLSEATRR DDVIKLFSVL TGTDDKLDVE ALDKELMTES HSIPASMLRS DEILLHPNFN
     RYHSETDMMR YMHRLERRDL ALNQAMIPLG SCTMKLNAAA EMLPISWPEF NELHPFCPPE
     QAQGYQQMIS QLSHWLVQLT GYDVVCMQPN SGAQGEYAGL LAIRRYHESR GEGHRHICLI
     PSSAHGTNPA SAHMAGMTVV VVSCDKEGNI DLVDLREKAE ESGNELSCIM VTYPSTHGVY
     EETIRQVCEI IHQYGGQVYL DGANMNAQVG ITAPGFIGAD VSHLNLHKTF CIPHGGGGPG
     MGPIGVKAHL APFLPGHSVV QMDGLTEQRA VSAAPFGSAS ILPISWMYIR MMGSQGLKQA
     SQTAILNANY IAARLKNDYD VLYTGHNGYV AHECILDIRP LKEEFGISEM DIAKRLIDYG
     FHAPTMSFPV AGTLMVEPTE SESKVEIDRF VDAMLAIRAE IGKVAKGEWS LEDNPLVNAP
     HVQAELVSDW SHSYSRETAV FPTLETKANK YWPAVKRLDD VYGDRNLHCS CAPVSDYQ