ID   GCSP_BURA4              Reviewed;         975 AA.
AC   B1YQQ1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=BamMC406_0143;
OS   Burkholderia ambifaria (strain MC40-6).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=398577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC40-6;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Ramette A.,
RA   Konstantinidis K., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia ambifaria MC40-6.";
RL   Submitted (APR-2008) 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=(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; CP001025; ACB62645.1; -; Genomic_DNA.
DR   RefSeq; WP_012362797.1; NC_010551.1.
DR   AlphaFoldDB; B1YQQ1; -.
DR   SMR; B1YQQ1; -.
DR   EnsemblBacteria; ACB62645; ACB62645; BamMC406_0143.
DR   KEGG; bac:BamMC406_0143; -.
DR   HOGENOM; CLU_004620_2_1_4; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000001680; Chromosome 1.
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.
FT   CHAIN           1..975
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000190207"
FT   MOD_RES         723
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   975 AA;  104289 MW;  93D43F60C3AB868C CRC64;
     MKLEHPDRLM NRTPLSLAAL ETHDAFAERH IGPDAASQQA MLDTLGFASR AALIDAVIPA
     SIRRAETLPL GPFAQPKSEA EALAALRALA DKNQVFRSYI GQGYHDTHTP AVILRNVLEN
     PAWYTAYTPY QPEISQGRLE ALLNFQQMVA DLTGLAISNA SLLDEATAAA EAMTLLQRTG
     KPASNVFYVA DDVLPQTLEV IRTRALPIGI EVKTGPAADA AQANAFGVLL QYPGVNGDVR
     DYRALTEAIH AAGGHVVVAA DLLALTVLTP PGEWGADVAV GNTQRFGVPM GFGGPHAAYL
     AVRDEFKRQM PGRLVGVTVD AQGKPALRLA LQTREQHIRR EKATSNVCTA QALLAIMASM
     YAVYHGPHGL KTIALRVNRI AALFAAGVKQ LGFATVNDTF FDTLTIDTGA RTAQVHEFAK
     ARRINLRRVS ATQVGVSFDE TTTRDDLAAL LAVFAQAAGG TAPSVDALDA GAAGVAALPA
     GLERTSAYLT HHVFNRHHSE TEMLRYLRSL SDKDLALDRS MIPLGSCTMK LNATSEMLPV
     TWPEFGRIHP FAPAEQTVGY REMIDQLEQM LVAATGYAAV SLQPNAGSQG EYAGLLIIHA
     YHASRGEAHR DVCLIPASAH GTNPASAHMA GMKVVVVACD AQGNVDIADL KAKAEQHAND
     LAAIMITYPS THGVFEQNVR EICEIVHAHG GQVYVDGANM NAMVGLTAPG QFGGDVSHLN
     LHKTFCIPHG GGGPGVGPVA VGAHLAKFLP NQRSTGYTRE EDGIGAVSAA PYGSASILPI
     SWMYIAMMGA KNLTAATETA ILNANYIAKR LAPHYPVLYS GPGGLVAHEC ILDLRPIKET
     SGISVDDVAK RLMDYGFHAP TMSFPVPGTL MVEPTESESQ EELDRFIAAM IAIREEIRAV
     EEGRADREDN PLRHAPHTAA VVTANEWPHA YSREQAAYPV ASLGTNKYWP PVGRADNAYG
     DRNLFCSCVP MSDYA