GCSP_BRUAB
ID GCSP_BRUAB Reviewed; 932 AA.
AC P62920; Q578K9; Q93MS6;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 98.
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=BruAb2_0506;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10858227; DOI=10.1128/iai.68.7.4102-4107.2000;
RA Hong P.C., Tsolis R.M., Ficht T.A.;
RT "Identification of genes required for chronic persistence of Brucella
RT abortus in mice.";
RL Infect. Immun. 68:4102-4107(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(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; AF396263; AAK73853.1; -; Genomic_DNA.
DR EMBL; AE017224; AAX75925.1; -; Genomic_DNA.
DR RefSeq; WP_002967268.1; NC_006933.1.
DR AlphaFoldDB; P62920; -.
DR SMR; P62920; -.
DR EnsemblBacteria; AAX75925; AAX75925; BruAb2_0506.
DR GeneID; 3828233; -.
DR KEGG; bmb:BruAb2_0506; -.
DR HOGENOM; CLU_004620_2_1_5; -.
DR OMA; CVPMSEY; -.
DR PRO; PR:P62920; -.
DR Proteomes; UP000000540; 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_0000166908"
FT MOD_RES 685
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
FT CONFLICT 42
FT /note="P -> S (in Ref. 1; AAK73853)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="P -> L (in Ref. 1; AAK73853)"
FT /evidence="ECO:0000305"
FT CONFLICT 930
FT /note="T -> A (in Ref. 1; AAK73853)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 932 AA; 99264 MW; 032D12EE4922B68D CRC64;
MTEFLPFVAR HIGPRHEDER AMLAALGLPS METLITQAVP APIRLNRALN 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 RHYHQARGQG 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 LICSCPPVAT YG
