ID   GCSP_PARPJ              Reviewed;         978 AA.
AC   B2T7I8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, 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=Bphyt_3882;
OS   Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS   (Burkholderia phytofirmans).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=398527;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17436 / LMG 22146 / PsJN;
RX   PubMed=21551308; DOI=10.1128/jb.05055-11;
RA   Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.;
RT   "Complete genome sequence of the plant growth-promoting endophyte
RT   Burkholderia phytofirmans strain PsJN.";
RL   J. Bacteriol. 193:3383-3384(2011).
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; CP001052; ACD18269.1; -; Genomic_DNA.
DR   RefSeq; WP_012434789.1; NC_010681.1.
DR   AlphaFoldDB; B2T7I8; -.
DR   SMR; B2T7I8; -.
DR   STRING; 398527.Bphyt_3882; -.
DR   KEGG; bpy:Bphyt_3882; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_4; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000001739; 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; 3.90.1150.10; 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:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 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..978
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000190211"
FT   MOD_RES         726
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   978 AA;  105136 MW;  B2DA4FFE230474A5 CRC64;
     MKLEHPDRLM NRTPLSLAAL EVHDAFAERH IGPDAADQHA MLEALGFASR AALIDAVIPK
     TIRRTETLPL GPFTQPKSEA EALAALRELA DKNQVFRSYI GQGYYNAHTP TVILRNVLEN
     PAWYTAYTPY QPEISQGRLE ALLNFQQMIV DLTGLAISNA SLLDEATAAA EAMTLLQRVG
     KPKSNVFFVA DDVLPQTIEV VRTRATPVGI EVKVGPASEA ANANAFGVLL QYPGVNGDVR
     DYRALTEAIH AAGGHVVVAA DLLALTVLTP PGEWGADVAV GNTQRFGVPV GFGGPHAAYL
     AVRDEFKRQM PGRLVGVTVD AQGNPALRLA LQTREQHIRR EKATSNVCTA QALLAIMASM
     YAVYHGPHGL KTIALRVNRI AALLAEGAKQ LGYTLANETF FDTLTFDTGA RTQALLDAAT
     AKRINLRRVS ATQVGLSIDE TTTRHDLADL LAVFAQAAFT NDVPQVDALD AKLAASNTAS
     VPAALERTSA YLTHHVFNRH HSETEMLRYL RSLSDKDLAL DRSMIPLGSC TMKLNATSEM
     LPVTWPEFGQ IHPFAPAEQT VGYREMIDQL EEMLVAATGY AAVSLQPNAG SQGEYAGLLI
     IHAYHASRGE AHRNVCLIPA SAHGTNPASA QMAGMQVVVV ACDAQGNVDI EDLKKKAGQH
     ADKLAAIMIT YPSTHGVFEQ NVREICEIVH AHGGQVYVDG ANMNAMVGLT APGQFGGDVS
     HLNLHKTFCI PHGGGGPGVG PVAVGAHLAQ FLPNQISSGY ERAPNGIGAV SGAPYGSASI
     LPISWMYIAM MGAKNLTAAT ETAILNANYV AKKLAPHYPV LYSGPGGLVA HECILDLRPI
     KETSGITVDD VAKRLADYGF HAPTMSFPVP GTLMVEPTES ESKEELDRFI EAMIAIREEI
     RAVEDGRSDR EDNPLKHAPH TAAVVIANDW KHAYARETAA YPLPTLIAKK YWPPVGRADN
     VYGDRNLFCS CVPIADYE
//