ID   GCSP_PROMH              Reviewed;         958 AA.
AC   B4F0N7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 89.
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}; OrderedLocusNames=PMI2019;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(2008).
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; AM942759; CAR44064.1; -; Genomic_DNA.
DR   RefSeq; WP_004248527.1; NC_010554.1.
DR   AlphaFoldDB; B4F0N7; -.
DR   SMR; B4F0N7; -.
DR   STRING; 529507.PMI2019; -.
DR   PRIDE; B4F0N7; -.
DR   EnsemblBacteria; CAR44064; CAR44064; PMI2019.
DR   GeneID; 6802088; -.
DR   KEGG; pmr:PMI2019; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   OMA; CVPMSEY; -.
DR   Proteomes; UP000008319; 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; -; 2.
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..958
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000132446"
FT   MOD_RES         708
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   958 AA;  105106 MW;  C3AB3A118C4BFCF5 CRC64;
     MTQTLTQLEY RDEFIRRHIG SSPEQIKEML DVVGISSLNE LTQKIVPDNI QLATPPNVGG
     GATEQEALAE LKAIARKNKR FTSYIGMGYA PSVLPPVILR NLLENPGWYT AYTPYQPEVS
     QGRLESLLNF QQVTIDYTGM DLASASLLDE ATAAAEAMAM AKRVSKLKNA ERFFVADDIH
     PQTLDVVKTR ANTFGFEVIV DKAEKVLELE GVFGVLLQQV GTTGEIHDYS QLISELKTRK
     IITSVAADLM ALVLLTAPGQ QGADIVLGSA QRFGVPMGYG GPHAAFFACR DEYKRAMPGR
     IIGVSRDAAG NRALRMAMQT REQHIRREKA NSNICTSQVL LANIAAMYAV YHGPEGLKNI
     AQRIHRLTDI LAAGLIQNGM TLRHQTWFDT LTVETADKAG VLQRAKDAEI NLRTDIVGAV
     GVTLSEVTTR EDVVRLIEII SGKAFSDDID TLDALVASSS TSIPTAMLRK DAVLTHENFH
     LYHSETEMMR YMHRLENKDL ALNQAMIPLG SCTMKLNAAA EMLPITWPEF TEMHPFCPPY
     QAQGYQIMIE QLSNWLAAIT GYDAMCMQPN SGAQGEYAGL LAIRRYHQSR GEGNRHICLI
     PSSAHGTNPA SAHMAGMTVV VVGCDENGNI DIADLKAKAE KHQAELSCVM VTYPSTHGVY
     EEGIREVCEI IHQYGGQVYL DGANMNAQVG ITTPGFIGSD VSHLNLHKTF CIPHGGGGPG
     MGPIGVKAHL APFVPGHSVV EMDGVTTQGA VSAAQFGSAS ILPISWMYIR MMGSEGLKQA
     SQVAILNANY IAQRLKDDYD ILYSGAEGYV AHECIIDIRP LKANYGISEM DVAKRLIDYG
     FHAPTMSFPV AGTLMIEPTE SESKVEIDRF IDALLSIRAE IAQVDDGVWP IDDNPLVNAP
     HTQYELVQEW SHSYSRECAV FPSEATKRNK YWPAVKRLDD VYGDRHLHCS CAPISDYE