ID   GCSP_CROS8              Reviewed;         957 AA.
AC   A7MR85;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 88.
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=ESA_00426;
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894;
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(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; CP000783; ABU75723.1; -; Genomic_DNA.
DR   RefSeq; WP_012123849.1; NC_009778.1.
DR   AlphaFoldDB; A7MR85; -.
DR   SMR; A7MR85; -.
DR   KEGG; esa:ESA_00426; -.
DR   PATRIC; fig|290339.8.peg.389; -.
DR   HOGENOM; CLU_004620_3_2_6; -.
DR   Proteomes; UP000000260; 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; 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; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..957
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045583"
FT   MOD_RES         708
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   957 AA;  104444 MW;  892D2C190C21BE41 CRC64;
     MTQTLSHLEN RDAFIERHIG PGVDQQQEML RTVGADSLDA LISQIVPADI QLATPPDVGD
     AATEFAALAE LKAIAGRNKR FKNYIGMGYT AVHTPPVILR NMLENPGWYT AYTPYQPEVS
     QGRLEALLNF QQVTLDLTGL DIASASLLDE ATAAAEAMAM AKRVSKLKNA NRFFVAADVH
     PQTLDVVRTR AETFGFEVIV DDAPKALDHQ DLFGVLLQQV GTTGEVHDYR ELISELKSRK
     VIVSVAADFM ALVLLTAPGK QGADIVFGSA QRFGVPMGYG GPHAAFFAAS DEFKRSMPGR
     IIGVSKDAAG RTALRMAMQT REQHIRREKA NSNICTSQVL LANIASLYAV FHGPAGLKRI
     ASRIHRFADI LAAGLQHKGL KLRHATWFDT LCVEVADKAT VLARAEASEI NLRSDIPGAV
     GITLDETTTR ADVQALLRVV TGEDATFDID ALDKEVAHDS RSIPAAMLRD DAILTHPVFN
     RYHSETEMMR YMHSLERKDL ALNQAMIPLG SCTMKLNAAA EMIPITWPEF AELHPFCPAD
     QAEGYLQMIS QLSDWLVKLT GYDALCMQPN SGAQGEYAGL LAIRHYHESR NEGHRDICLI
     PSSAHGTNPA SAQMAGMQVV VVACDKQGNI DLADLRAKAE TAGDKLSCIM VTYPSTHGVY
     EETIREVCDI VHQYGGQVYL DGANMNAQVG ITSPGYIGAD VSHLNLHKTF CIPHGGGGPG
     MGPIGVKAHL APFVPGHSVV QIEGMLTSQG AVSAAPFGSA SILPISWMYI RMMGSQGLKK
     ASQTAILNAN YIASRLKDAY PVLYTGRDGR VAHECILDIR PLKEATGISE LDIAKRLIDY
     GFHAPTMSFP VAGTLMVEPT ESESKVELDR FIDAMLAIRG EIDRVAQGEW PQDDNPLVNA
     PHVQRELAQE WEHAYSRELA AFPAGFENKY WPTVKRLDDV YGDRNLFCSC VPMSEYQ
//