ID   GCSP_PARXL              Reviewed;         978 AA.
AC   Q13SR6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 106.
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=Bxeno_A4335; ORFNames=Bxe_A0054;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000270; ABE32873.1; -; Genomic_DNA.
DR   RefSeq; WP_011490275.1; NZ_CP008760.1.
DR   AlphaFoldDB; Q13SR6; -.
DR   SMR; Q13SR6; -.
DR   STRING; 266265.Bxe_A0054; -.
DR   KEGG; bxb:DR64_2233; -.
DR   KEGG; bxe:Bxe_A0054; -.
DR   PATRIC; fig|266265.5.peg.4557; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000001817; 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_1000045578"
FT   MOD_RES         726
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   978 AA;  105253 MW;  7B74B5CD79035C11 CRC64;
     MKLEHPDRLM NRTPLSLAAL EVHDAFAERH IGPDSADQQA MLEALGFASR AALIDAVIPK
     TIRRTEPLPL GPFAQPKSEA EALATLRELA DRNQVFRSYI GQGYYNAHTP TVILRNVLEN
     PAWYTAYTPY QPEISQGRLE ALLNFQQMIV DLTGLAISNA SLLDEATAAA EAMTLLQRIG
     KPKSNVFYVA DDVLPQTIEV VKTRATPVGI EVKVGPAADA ANANAFGVLL QYPGVNGDVR
     DYRALAEAIH AAGGHVVVAA DLLALTVLTP PGEWGADVAV GNTQRFGVPV GFGGPHAAYL
     AVRDEFKRQM PGRLVGVTVD AQGNPALRLA LQTREQHIRR EKATSNVCTA QALLAIMASM
     YAVYHGPHGL KTIALRVNRI AALLAEGAKQ LGYTLVNETF FDTLTFETGA RTQALHDAAL
     AKRINLRRVS DTQVGLSVDE TTTRRDLADL LEVFAQAAGA KIVPQVDALD STIAASDTAS
     VPPALERTSA YLTHHVFNRH HSETEMLRYL RSLSDKDLAL DRSMIPLGSC TMKLNATSEM
     LPVTWPEFGQ IHPFAPAEQT VGYREMIDQL EAMLVAATGY AAVSLQPNAG SQGEYAGLLI
     IHAYHASRGE AHRNVCLIPA SAHGTNPASA HMAGMQVIVV ACDAQGNVDI EDLKKKAEQH
     ADKLAAIMIT YPSTHGVFEQ NVREICEIVH AHGGQVYVDG ANMNAMVGLT APGQFGGDVS
     HLNLHKTFCI PHGGGGPGVG PVAVGAHLAQ FLPNQISSGY ERAPNGIGAV SGAPYGSASI
     LPISWMYIAM MGAKNLTAAT ETAILNANYV AKKLAPHYPV LYSGPGGLVA HECILDLRPI
     KETSGITVDD VAKRLADYGF HAPTMSFPVP GTLMVEPTES ESKEELDRFI EAMIAIREEI
     RAVEEGRSDR EDNPLKHAPH TAAVVIANDW KHAYARETAA YPLPTLIAKK YWPPVGRADN
     VYGDRNLFCS CVPIADYE
//