ID   GCSP_KLEP7              Reviewed;         957 AA.
AC   A6TDR5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=KPN78578_32750; ORFNames=KPN_03339;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) 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: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; CP000647; ABR78736.1; -; Genomic_DNA.
DR   RefSeq; WP_015958957.1; NC_009648.1.
DR   AlphaFoldDB; A6TDR5; -.
DR   SMR; A6TDR5; -.
DR   STRING; 272620.KPN_03339; -.
DR   jPOST; A6TDR5; -.
DR   EnsemblBacteria; ABR78736; ABR78736; KPN_03339.
DR   KEGG; kpn:KPN_03339; -.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   OMA; CVPMSEY; -.
DR   Proteomes; UP000000265; 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..957
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045586"
FT   MOD_RES         708
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   957 AA;  104553 MW;  20AE60CF45FFCB3E CRC64;
     MTQTLSQLEN RDAFIERHIG PDAQQQQEML KTVGADSLNA LIGQIVPQDI QLATPPQVGD
     ATTEFAALAE LKAIASRNKR FKSYIGMGYT AVQLPPVIQR NMLENPGWYT AYTPYQPEVS
     QGRLESLLNF QQVTLDLTGL DIASASLLDE ATAAAEAMAM AKRVSKLKSA NRFFVAADVH
     PQTLDVVRTR AETFGFDVIV DDADKVLDHQ DVFGVLLQQV GTTGEIHDYS KLIAELKARK
     VIVSVAADFM ALVLLTAPGK QGADIVFGSA QRFGVPMGYG GPHAAFFAAK DEFKRSMPGR
     IIGVSKDAAG NTALRMAMQT REQHIRREKA NSNICTSQVL LANIASLYAV FHGPAGLKRI
     AGRIHRLTDI LADGLQKKGL KLRHAHYFDT LCVEVADKAA VLARAEALQI NLRSDIHGAV
     GITLDEATTR EDVLNLFRAI VGDDHGLDID TLDKDVALDS RSIPAAMLRD DAILTHPVFN
     RYHSETEMMR YMHALERKDL ALNQAMIPLG SCTMKLNAAA EMIPITWPEF AELHPFCPVE
     QAEGYQQMIA QLSDWLVKLT GYDAVCMQPN SGAQGEYAGL LAIRHYHESR NEGHRDICLI
     PSSAHGTNPA SAQMAGMQVV VVACDKNGNI DLADLREKAE QAGANLSCIM VTYPSTHGVY
     EETIREVCEI VHQFGGQVYL DGANMNAQVG ITSPGFIGAD VSHLNLHKTF CIPHGGGGPG
     MGSIGVKAHL APFVPGHSVV QIEGMLTRQG AVSAAPFGSA SILPISWMYI RMMGAEGLKQ
     ASQNAILNAN YIATRLKDAY PVLYTGRDGR VAHECILDIR PLKEETGISE LDIAKRLIDF
     GFHAPTMSFP VAGTLMVEPT ESESKVELDR FIDAMLAIRA EIDRVKAGEW PLEDNPLVNA
     PHTQGELVGE WNHPYSRELA VFPAGLHNKY WPTVKRLDDV YGDRNLFCSC VPMSEYQ