ID   GCSP_ENT38              Reviewed;         957 AA.
AC   A4WE55;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 103.
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=Ent638_3322;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638;
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(2010).
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; CP000653; ABP61985.1; -; Genomic_DNA.
DR   RefSeq; WP_015960313.1; NC_009436.1.
DR   AlphaFoldDB; A4WE55; -.
DR   SMR; A4WE55; -.
DR   STRING; 399742.Ent638_3322; -.
DR   KEGG; ent:Ent638_3322; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_6; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000000230; 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
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..957
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000062076"
FT   MOD_RES         708
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   957 AA;  104745 MW;  3F6EAAD4B561D2B5 CRC64;
     MTQTLSQLEN RGAFIERHIG PDAQQQQEML KTVGADSLNA LIGQIVPKDI QLATPPQVGE
     ATTEFAALAE LKAIAGLNKR FKSYIGMGYT PVQLPPVILR NMLENPGWYT AYTPYQPEVS
     QGRLEALLNF QQVTLDLTGL DIASASLLDE ATAAAEAMAM AKRVSKLKNA NRFFVAADVH
     PQTLDVVRTR AETFGFDVIV DDADKVLDHQ DVFGVLLQQV GTTGEVHDYS ALISELKSRK
     IIVSVAADFM ALVLLTAPGK QGADIVFGSA QRFGVPMGYG GPHAAFFAGK DEFKRSMPGR
     IIGVSKDAAG NTALRMAMQT REQHIRREKA NSNICTSQVL LANIASLYAV FHGPVGLKRI
     ATRIHRFADI LATGLQQKGL KLRHAHYFDT LCVEVADKAG VLARAEAAEI NLRSDILNAV
     GITLDETTTR EDVQNLFNVL LGDAHGLDVD ALDKEVAHDS RSIQESMLRD DAILSHPVFN
     RHHSETEMMR YMHSLERKDL ALNQAMIPLG SCTMKLNAAA EMIPITWPEF SELHPFCPAD
     QAEGYHQMIN QLSDWLVKLT GYDALCMQPN SGAQGEYAGL LAIRHYHESR NEGHRDICLI
     PSSAHGTNPA SAQMAGMEVV VVACDKNGNI DLTDLRAKAE HAGEKLSCIM VTYPSTHGVY
     EETIREVCEI VHQFGGQVYL DGANMNAQVG ITSPGFIGAD VSHLNLHKTF CIPHGGGGPG
     MGPIGVKAHL APFVPGHSVV QIEGMLTRQG AVSAAPFGSA SILPISWMYI RMMGAEGLKQ
     ASQVAILNAN YIATRLKDAY PVLYTGRDGR VAHECILDIR PLKDDTGISE LDIAKRLIDY
     GFHAPTMSFP VAGTLMVEPT ESESKVELDR FIEAMLAIRH EITRVKQGEW TLEDNPLVNA
     PHTQNELVAE WHHGYTREVA VFPAGMANKY WPTVKRLDDV YGDRNLFCSC VPMSEYQ
//