ID   GCSP_BDEBA              Reviewed;         958 AA.
AC   Q6MPZ6;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 100.
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=Bd0692;
OS   Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS   HD100).
OC   Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC   Bdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=264462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX   PubMed=14752164; DOI=10.1126/science.1093027;
RA   Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA   Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA   Schuster S.C.;
RT   "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT   genomic perspective.";
RL   Science 303:689-692(2004).
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; BX842647; CAE78651.1; -; Genomic_DNA.
DR   RefSeq; WP_011163253.1; NC_005363.1.
DR   AlphaFoldDB; Q6MPZ6; -.
DR   SMR; Q6MPZ6; -.
DR   STRING; 264462.Bd0692; -.
DR   PRIDE; Q6MPZ6; -.
DR   EnsemblBacteria; CAE78651; CAE78651; Bd0692.
DR   KEGG; bba:Bd0692; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_2_1_7; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000008080; 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_0000227095"
FT   MOD_RES         705
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   958 AA;  104226 MW;  A21D228C935F7991 CRC64;
     MKIADLSPTN EFIPRHIGPT DSDIHEMLKT LGFNSLDQMA DKVIPAQIRT THAYADVGNG
     ISEHGLLNHL KQMVSKNKVY KNYIGMGYHD TITPTVIQRN IFENPVWYTA YTPYQPEISQ
     GRLEALLNFQ TMIADLNGME IANASLLDEG TAAAEAMFMA HSLCKNKANA FVVSPDMHPH
     VIEVIGTRAE PLGFEMIVMD PAKYDFAKPV FGVFFQYPNT NGTVEDYAAI AKKYKDHGAL
     VTASTDLLAM TLLTPPGEWG ADMVVGNSQR FGVPLGFGGP HAGFLATKDA FKRLMPGRLV
     GVSVDSQGKS ALRLALQTRE QHIRREKATS NICTAQVLLA NMASMYAVYH GPAGLKKIAL
     RVQRLTAILS AGLKKLNLEV GAGHVFDTVT VKTDKAAEII AQAEKMQMNF RNYGGGKLGV
     SLNEATTLED VEQIWAAFNL GKAAGFTALS VDESLADVTL PANLTRSTAY MTHQVFNSHH
     SETEMLRYIH HLQNKDLTLT HSMIPLGSCT MKLNATTELV PVSWPEISKL HPFAPTAQAV
     GLIEMIHDLE KKLCDITGFA AVSLQPNAGS QGEYAGLLVI RKYHQSRGQG HRNICLIPSS
     AHGTNPASAA LVNMQVVVVA CDDQGNVDVA DLKAKAEQHK DNLAALMITY PSTHGVFEEG
     IVEICKIIHD NGGQVYMDGA NMNALVGMCR PGVFGPDVSH MNLHKTFSIP HGGGGPGVGP
     IGVGAHLAEF LPKHSLVPEA GPANGISATT SAPWGSASIL PISWAYITMM GAQGLRKATL
     VSILSANYIA KKLEAHYPVL YKGKNGLVAH ECIVDVREIK KTSGIDVTDV AKRLMDFGFH
     APTMSFPVAG TLMIEPTESE SKKELDRFIE SMVTIRKEIA AVETGKMDKE NNALKNAPHT
     AQMLMKPEWN HPYSREEAVY PVEWLRGNKF WPVVGRVDNA YGDRNLICSC PSIEDYQA