GCSP_BURPS
ID GCSP_BURPS Reviewed; 975 AA.
AC Q63PL2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=BPSL3362;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(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; BX571965; CAH37375.1; -; Genomic_DNA.
DR RefSeq; WP_004195877.1; NZ_CP009538.1.
DR RefSeq; YP_109957.1; NC_006350.1.
DR AlphaFoldDB; Q63PL2; -.
DR SMR; Q63PL2; -.
DR STRING; 272560.BPSL3362; -.
DR PRIDE; Q63PL2; -.
DR EnsemblBacteria; CAH37375; CAH37375; BPSL3362.
DR GeneID; 56594511; -.
DR KEGG; bps:BPSL3362; -.
DR PATRIC; fig|272560.51.peg.1838; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR OMA; CVPMSEY; -.
DR Proteomes; UP000000605; 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; Reference proteome.
FT CHAIN 1..975
FT /note="Glycine dehydrogenase (decarboxylating)"
FT /id="PRO_0000227098"
FT MOD_RES 723
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ SEQUENCE 975 AA; 104460 MW; F610AD40C9512103 CRC64;
MKLEHPDRLM NRTPLSLAAL ETHDAFAERH IGPDAASQQA MLDTLGFATR AALIDAVIPA
SIRRAETLPL GPFAQPKSEA EALAALRALA DKNQVFRSYI GQGYYDTHTP AVILRNVLEN
PAWYTAYTPY QPEISQGRLE ALLNFQQMVA DLTGLEISNA SLLDEATAAA EAMTLLQRVG
KPQSNVFYVA DDVLPQTLEV IKTRAKPIGI EVKSGPAADA AAANAFGVLL QYPGANGDVR
DYRALADAIH AAGGHVVVAA DILALTVLMP PGEWGADVAV GNTQRFGVPM GFGGPHAAYM
AVRDEFKRQM PGRLVGVTVD AQGKPALRLA LQTREQHIRR EKATSNVCTA QALLAIMASM
YAVYHGPRGL KTIALRVNRI AALLAAGIRH LGYATVNDTF FDTLTIDTGA RTAQLHAFAQ
AKRINLRRAG DTRVGVSVDE TTTRADLADL LTIFAQAAGA TAPDIDALDA GLLPAPALPP
SLERTSAYLT HHVFNRHHSE TEMLRYLRSL SDKDLALDRS MIPLGSCTMK LNATSEMLPV
TWPEFGRIHP FAPAEQTVGY REMIDQLEQM LVAATGYAAV SLQPNAGSQG EYAGLLIIHA
YHESRGESHR DVCLIPASAH GTNPASAHMA GMKVVVVACD AQGNVDIADL KAKADAHSHD
LAAIMITYPS THGVFEQNVR EICEIVHAHG GQVYVDGANM NAMVGLTAPG QFGGDVSHLN
LHKTFCIPHG GGGPGVGPVA VGPHLAKFLP NQRSTGYARG EDGIGAVSAA PYGSASILPI
SWMYIAMMGA KNLTAATETA ILNANYIAKR LAPHYPVLYS GPGGLVAHEC ILDLRPIKDS
SGITVDDVAK RLMDYGFHAP TMSFPVPGTL MVEPTESESQ EELDRFIAAM IAIRDEIRAV
EEGRADREDN PLRHAPHTAA VVTANEWPHA YSREQAAFPV ASLVANKYWP PVGRADNAYG
DRNLFCSCVP VSDYA
