GCSP_BRUSU
ID GCSP_BRUSU Reviewed; 932 AA.
AC Q8FVU9; G0KD95;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 104.
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=BRA0725, BS1330_II0718;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(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=(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; AE014292; AAN33907.1; -; Genomic_DNA.
DR EMBL; CP002998; AEM20183.1; -; Genomic_DNA.
DR RefSeq; WP_004690267.1; NZ_KN046805.1.
DR AlphaFoldDB; Q8FVU9; -.
DR SMR; Q8FVU9; -.
DR EnsemblBacteria; AEM20183; AEM20183; BS1330_II0718.
DR GeneID; 45053745; -.
DR KEGG; bms:BRA0725; -.
DR KEGG; bsi:BS1330_II0718; -.
DR PATRIC; fig|204722.21.peg.2344; -.
DR HOGENOM; CLU_004620_2_3_5; -.
DR OMA; CVPMSEY; -.
DR PhylomeDB; Q8FVU9; -.
DR PRO; PR:Q8FVU9; -.
DR Proteomes; UP000007104; Chromosome II.
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..932
FT /note="Glycine dehydrogenase (decarboxylating)"
FT /id="PRO_0000166910"
FT MOD_RES 685
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ SEQUENCE 932 AA; 99254 MW; E3889FEE67C92252 CRC64;
MTEFLPFVAR HIGPRHEDER AMLAALGLPS METLITQAVP ASIRLNRALN LPAALSEADA
LAELGTIMGR NVVKKSFIGA GYHGVHTPPV IQRNLFENPA WYTAYTPYQS EISQGRLELL
FHFQTLVAEL TGLPVACASL LDEATAVAEA IGVACRHHRD KRSRILLAGE LHPQTVDVVN
TRAEPLGWEI ATGSDVDDNT AAIVVPWPDT RGVYGDFAKV IADAKAKGAL VIAVADPLAL
TIMEAPARWG ADMAVGSMQR YGVPMGFGGP HAAYLAVSEA LTRIIPGRIV GQSVDAHGRA
AYRLALQTRE QHIRRDKATS NICTAQALLA NMAAAFAIWH GPAGLQAIAT RVAALAARFA
AALKAAGVEI AGESLFDTVT AKVPGKAAAI AAEADKGGRL IRIIDADTVG VTFDETSTEE
DLTALASLFG AKPVGGDTVL VPGKERGEGF LTQEVFHSHR SETEMMRFLR RLADKDLALD
RAMIPLGSCT MKLNAAAEMM PVSWNTVANL HPFAPAEQVQ GYAKMTSDLE AWLCEITGFA
GVSLQPNAGS QGEYAGLMAI RHYHQAWGQG HRNICLIPSS AHGTNPASAS MAGMSVVVVN
CRPDGDIDID DLKAKAEKHR DNLAAFMITY PSTYGVFEEG IKAFCEIVHD NGGQVYFDGA
NLNALVGLAR PADIGADVCH MNLHKTFCIP HGGGGPGVGP IGVAKHLVPY LPGHVEAGSE
HAVAAAQFGS ASILVITWMY IRMMGGAGLK KATEAAILNA NYIAHRLKGV YPILYTGAHD
RVAHECIVDT RVLKDSAGIT VEDVAKRLID YGFHAPTMSW PVAGTLMIEP TESEPKLEID
RLCDAMIAIA GEAKKVADGV WPADDNPLAN APHTASDTLA TEWKHPYTRE EAVFPGGAFD
PTAKYWPPVS RVDNVGGDRN LICSCPPVAA YG
