ID   GCSP_BRUMB              Reviewed;         932 AA.
AC   C0RLN1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=BMEA_B0701;
OS   Brucella melitensis biotype 2 (strain ATCC 23457).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=546272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23457;
RA   Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J.,
RA   Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E.,
RA   Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C., Tapia R.,
RA   Han C., Detter J.C., Bruce D., Brettin T.S.;
RT   "Brucella melitensis ATCC 23457 whole genome shotgun sequencing project.";
RL   Submitted (MAR-2009) 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=(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; CP001489; ACO02514.1; -; Genomic_DNA.
DR   RefSeq; WP_004684905.1; NC_012442.1.
DR   AlphaFoldDB; C0RLN1; -.
DR   SMR; C0RLN1; -.
DR   EnsemblBacteria; ACO02514; ACO02514; BMEA_B0701.
DR   KEGG; bmi:BMEA_B0701; -.
DR   HOGENOM; CLU_004620_2_1_5; -.
DR   OMA; CVPMSEY; -.
DR   PRO; PR:C0RLN1; -.
DR   Proteomes; UP000001748; 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_1000147962"
FT   MOD_RES         685
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   932 AA;  99223 MW;  AE3FEFEC17C9997C 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 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 LICSCPPVAA YG