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 27-MAR-2024, entry version 91.
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; Pseudomonadota; 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=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; 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 PaxDb; 272620-KPN_03339; -.
DR EnsemblBacteria; ABR78736; ABR78736; KPN_03339.
DR KEGG; kpn:KPN_03339; -.
DR HOGENOM; CLU_004620_1_1_6; -.
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; 3.90.1150.10; 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_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
//
