ID GCSP_BURM1 Reviewed; 975 AA.
AC A9ACU3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 100.
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=Bmul_0141, BMULJ_03124;
OS Burkholderia multivorans (strain ATCC 17616 / 249).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=395019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC
RT 17616.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA Hattori M., Tsuda M.;
RT "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL Submitted (APR-2007) 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=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; CP000868; ABX13836.1; -; Genomic_DNA.
DR EMBL; AP009385; BAG44998.1; -; Genomic_DNA.
DR RefSeq; WP_012212498.1; NC_010804.1.
DR AlphaFoldDB; A9ACU3; -.
DR SMR; A9ACU3; -.
DR STRING; 395019.BMULJ_03124; -.
DR KEGG; bmj:BMULJ_03124; -.
DR KEGG; bmu:Bmul_0141; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_1_1_4; -.
DR Proteomes; UP000008815; 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; Reference proteome.
FT CHAIN 1..975
FT /note="Glycine dehydrogenase (decarboxylating)"
FT /id="PRO_1000190210"
FT MOD_RES 723
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ SEQUENCE 975 AA; 104329 MW; B67BC9F13ED99B36 CRC64;
MKLEHPDRLM NRTPLSLAAL ETHDAFAERH IGPDAASQQA MLDTLGFASR AALIDAVIPA
SIRRNETLPL GPFSQPKSEA EALAALRALA DKNQVFRSYI GQGYYDTHTP AVILRNVLEN
PAWYTAYTPY QPEISQGRLE ALLNFQQMVT DLTGLAISNA SLLDEATAAA EAMTLLQRVG
KPKSNVFYVA DDVLPQTLEV IRTRALPIGI DVKTGPAADA AQSNAFGVLL QYPGVNGDVR
DYRALTDAIH AAGGHVVVAA DLLALTVLTP PGEWGADVAV GNTQRFGVPM GFGGPHAAYL
AVRDEFKRQM PGRLVGVTVD AQGKPALRLA LQTREQHIRR EKATSNVCTA QALLAIMASM
YAVYHGPHGL KTIALRVNRI AALFAAGVKQ LGFATVNDTF FDTVTVDTGA RTAQVHAFAN
AKRINLRRVS DARVGVSIDE TTTRDDLADL LAVFAQAAGG TAPSVDALDA GLGGEAALPA
SLVRTSAYLT HHVFNRHHSE TEMLRYLRSL SDKDLALDRS MIPLGSCTMK LNATSEMLPV
TWPEFGRIHP FAPAEQTVGY REMIDQLEQM LVAATGYAAV SLQPNAGSQG EYAGLLIIHA
YHASRGEGHR DVCLIPASAH GTNPASAHMA GMKVVVVACD AQGNVDIADL KAKAEQHSAN
LAAIMITYPS THGVFEQNVR EICEIVHAHG GQVYVDGANM NAMVGLTAPG QFGGDVSHLN
LHKTFCIPHG GGGPGVGPVA VGAHLAKFLP NQRSTGYTRG EDGIGAVSAA PYGSASILPI
SWMYIAMMGA KNLTAATETA ILNANYIAKR LAPHYPVLYS GPGGLVAHEC ILDLRPIKES
SGITVDDVAK RLMDYGFHAP TMSFPVPGTL MVEPTESESK EELDRFIDAM IAIRDEIRAV
EEGRADREDN PLRHAPHTAA VVTANEWPHA YSREQAAYPV ASLGTNKYWP PVGRADNAYG
DRNLFCACVP MSDYA
//
