ID   GCSP_PECCP              Reviewed;         956 AA.
AC   C6D8X1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 81.
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=PC1_0624;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) 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; CP001657; ACT11679.1; -; Genomic_DNA.
DR   RefSeq; WP_012773326.1; NC_012917.1.
DR   AlphaFoldDB; C6D8X1; -.
DR   SMR; C6D8X1; -.
DR   STRING; 561230.PC1_0624; -.
DR   KEGG; pct:PC1_0624; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_6; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000002736; 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.
FT   CHAIN           1..956
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000212655"
FT   MOD_RES         708
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   956 AA;  103905 MW;  27B74740AAB76B49 CRC64;
     MTQTLSQLEH DGAFIERHIG PSVSQQQHML SVVGATSLDA LIRQIVPQDI QLPSPPAVGE
     AATEHEALSE LKAIAGRNQR YKSYIGMGYS AVLMPPVILR NVLENPGWYT AYTPYQPEVS
     QGRLEALLNF QQVTQDLTGL DLASASLLDE ATAAAEAMAM AKRISKLKQA ERFFVADDVH
     PQTLDVVRTR AETFGFEIVV GKAEDALKDD AVFGVLLQQV GTTGELHDYS DLMAALKARK
     VVSCVASDIM ALVLLTAPGK QGADIVFGSA QRFGVPMGYG GPHAAFFACR DEHKRAMPGR
     IIGVSRDAAG NTALRMAMQT REQHIRREKA NSNICTSQVL LANIAGMYAV FHGPEGLKRI
     AGRIHRLTDI LAAGLTQGGL LLRHRSWFDT LTIEVADKDA VLSRALSFGI NLRSDLASAV
     GITLDEATTR EDVLALFAVL LGDDHGLDIG ALDAAISQQA ATIPAGLLRQ DAILSHPVFN
     RYHSETEMMR YLHRLARKDL ALNQAMIPLG SCTMKLNAAA EMLPITWPEF AELHPFCPPE
     QALGYRQMIE QLSGWLVQLT GYDAICMQPN SGAQGEYAGL LAIRRYHESR NEAGRHLCLI
     PSSAHGTNPA SAQMAGMDVV VVACDKQGNI DLHDLREKAQ AAGEQLSCIM VTYPSTHGVY
     EETIREVCQI VHQYGGQVYL DGANMNAQVG ITTPGYIGAD VSHLNLHKTF CIPHGGGGPG
     MGPIGVKAHL APFVPGHQVV KIDGVLTEQG AVSAAPFGSA SILPISWMYI RMMGAEGLKQ
     ASQMAILNAN YIATRLQQAY PVLYTGRDGR VAHECILDIR PLKESTGISE MDIAKRLIDY
     GFHAPTMSFP VAGTLMVEPT ESESQVEIDR FVDAMLAIRA EINRVAQGEW PLDDNPLVNA
     PHTQAELVAD WAHPYSRELA VFPAGSEHKY WPSVKRLDDV YGDRNLFCSC VPMSDY
//