ID   GCSP_BRUME              Reviewed;         932 AA.
AC   P62921; Q93MS6;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 105.
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=BMEII0561;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AE008918; AAL53803.1; -; Genomic_DNA.
DR   PIR; AH3579; AH3579.
DR   RefSeq; WP_004682032.1; NZ_GG703779.1.
DR   AlphaFoldDB; P62921; -.
DR   SMR; P62921; -.
DR   GeneID; 29595431; -.
DR   KEGG; bme:BMEII0561; -.
DR   KEGG; bmel:DK63_2685; -.
DR   PATRIC; fig|224914.52.peg.2813; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   PhylomeDB; P62921; -.
DR   Proteomes; UP000000419; 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_0000166909"
FT   MOD_RES         685
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   932 AA;  99240 MW;  DE3FEFEA2FDCCC29 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 AKLVGGDTVL 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
//