ID   GCSP_BURTA              Reviewed;         975 AA.
AC   Q2STK2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=BTH_I3253;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS   E264).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
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; CP000086; ABC38436.1; -; Genomic_DNA.
DR   RefSeq; WP_009910201.1; NZ_CP008785.1.
DR   AlphaFoldDB; Q2STK2; -.
DR   SMR; Q2STK2; -.
DR   PRIDE; Q2STK2; -.
DR   EnsemblBacteria; ABC38436; ABC38436; BTH_I3253.
DR   KEGG; bte:BTH_I3253; -.
DR   HOGENOM; CLU_004620_2_1_4; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000001930; Chromosome I.
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_1000045576"
FT   MOD_RES         723
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   975 AA;  104360 MW;  36FA585C545A4BB3 CRC64;
     MKLEHPDRLM KRTPLSLAAL ETHDAFAERH IGPDAASQQA MLDTLGFATR AALIDAVIPA
     SIRRAETLPL GPFAQPLSEA EALAALRELA DKNQVFRSYI GQGYYDTHTP AVILRNVLEN
     PAWYTAYTPY QPEISQGRLE ALLNFQQMVA DLTGLEISNA SLLDEATAAA EAMTLLQRVG
     KPQSNVFYVA DDVLPQTLEV IKTRAKPIGI EVKSGPAADA AAANAFGVLL QYPGVNGDVR
     DYRALADAIH AAGGHVVVAA DILALTVLTP PGEWGADVAV GNTQRFGVPM GFGGPHAAYM
     AVRDEFKRQM PGRLVGVTVD AQGKPALRLA LQTREQHIRR EKATSNVCTA QALLAIMASM
     YAVYHGPRGL KTIALRVNRI AALVAAGVKQ LGFATVNDTF FDTLTIDTGA RTAQIHALAN
     AKRINLRRVS DTRVGISVDE TTTRGDLAEL LGVFAQAAGG TAPDVDALDA GLADTAALPA
     GLQRTSAYLT HHVFNRHHSE TEMLRYLRSL SDKDLALDRS MIPLGSCTMK LNATSEMLPV
     TWPEFGRIHP FAPAEQTVGY REMIDQLEQM LVAATGYAAV SLQPNAGSQG EYAGLLIIHA
     YHESRGESHR NVCLIPASAH GTNPASAHMA GMKVVVVACD AQGNVDIDDL KAKAEQHAND
     LAAIMITYPS THGVFEQNVR EICEIVHAHG GQVYVDGANM NAMVGLTAPG QFGGDVSHLN
     LHKTFCIPHG GGGPGVGPVA VGAHLAKFLP NQRSTGYARA EDGIGAVSAA PYGSASILPI
     SWMYIAMMGA KNLTAATETA ILNANYIAKR LAPHYPVLYS GPGGLVAHEC ILDLRPIKDS
     SGITVDDVAK RLMDYGFHAP TMSFPVPGTL MVEPTESESQ EELDRFVAAM IAIRDEIRAV
     EEGRADREDN PLRHAPHTAA VVTANEWPHA YSREQAAYPV ASLVANKYWP PVGRADNAYG
     DRNLFCSCVP VSDYA