ID GCSP_BRUO2 Reviewed; 932 AA.
AC A5VV25;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
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=BOV_A0679;
OS Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=444178;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25840 / 63/290 / NCTC 10512;
RX PubMed=19436743; DOI=10.1371/journal.pone.0005519;
RA Tsolis R.M., Seshadri R., Santos R.L., Sangari F.J., Lobo J.M.,
RA de Jong M.F., Ren Q., Myers G., Brinkac L.M., Nelson W.C., Deboy R.T.,
RA Angiuoli S., Khouri H., Dimitrov G., Robinson J.R., Mulligan S.,
RA Walker R.L., Elzer P.E., Hassan K.A., Paulsen I.T.;
RT "Genome degradation in Brucella ovis corresponds with narrowing of its host
RT range and tissue tropism.";
RL PLoS ONE 4:E5519-E5519(2009).
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; CP000709; ABQ62542.1; -; Genomic_DNA.
DR RefSeq; WP_006016275.1; NC_009504.1.
DR AlphaFoldDB; A5VV25; -.
DR SMR; A5VV25; -.
DR GeneID; 45126057; -.
DR KEGG; bov:BOV_A0679; -.
DR HOGENOM; CLU_004620_3_2_5; -.
DR PhylomeDB; A5VV25; -.
DR PRO; PR:A5VV25; -.
DR Proteomes; UP000006383; 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; 3.90.1150.10; 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.
FT CHAIN 1..932
FT /note="Glycine dehydrogenase (decarboxylating)"
FT /id="PRO_1000045567"
FT MOD_RES 685
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ SEQUENCE 932 AA; 99298 MW; 901F425F7E9A5AB7 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 HAAYLAVSEV LTRIIPGRIV GQSVDAHGRA
AYRLALQTRE QHIRRDKATS NICTAQALLA NMAAAFAIWH GPAGLQAIAM RVAALAARFA
AALKAAGVEI AGESLFDTVT AKVPGKAAAI AAEADKGGRL IRIIDTDTVG VTFDETSTEE
DLTALASLFG TKPVGGDTVL 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 TEWKHPYTRA EAIFPGGAFD
PTAKYWPPVS RVDNVGGDRN LICSCPPVAA YG
//
