ID   GCSP_BORA1              Reviewed;         955 AA.
AC   Q2KYL7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=BAV0493;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N;
RX   PubMed=16885469; DOI=10.1128/jb.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ48098.1; -; Genomic_DNA.
DR   RefSeq; WP_012416189.1; NC_010645.1.
DR   AlphaFoldDB; Q2KYL7; -.
DR   SMR; Q2KYL7; -.
DR   STRING; 360910.BAV0493; -.
DR   EnsemblBacteria; CAJ48098; CAJ48098; BAV0493.
DR   GeneID; 41392404; -.
DR   KEGG; bav:BAV0493; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_2_1_4; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000001977; Chromosome.
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; Reference proteome.
FT   CHAIN           1..955
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045566"
FT   MOD_RES         702
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   955 AA;  102819 MW;  93E0C5A398CC62FD CRC64;
     MSRALDTHSD FIPRHIGPSE ADQAKMLATI GCSSLDALLE EVVPPRIRNQ APLALPGARS
     EPDVLAELKQ MAARNKVFRN YIGQGYYGTH TPNVVLRNVL ENPAWYTAYT PYQPEISQGR
     LEALLNYQTM VADLTGLDIS NASLLDEGTA AAEAMTLARR SAKSKSAVFF VSQHCHPQTI
     EVVRTRAQGL DIDVLVGDES QGLPECFGVL LQYPHSLGGV VNYRELAEAA HAQGAVVACA
     TDLLALALLT PPGEWGADIA VGTAQRFGVP FGFGGPHAGF MACRDAFKRN MPGRLVGVSK
     DAQGNPALRL ALQTREQHIR REKATSNICT AQVLLAVMAG LYAVWHGPAG LRRIATRVHT
     FAGVLRQHVQ ALGLTVENDS YFDTLLINTG PATPAVLRAA ECAHINLRRV DAGRVAVSID
     ETVTVEDLQA LINVFAAGLG KDDITLDAAT LAPEAGLPAG TVRTSPILSH PVFSSVQSET
     DMLRYLRKLA DKDLALDRSM IPLGSCTMKL NATAEMIPIT WPEFALIHPF APADQTAGYR
     ELIERLSAAL CEITGYDNIS LQPNSGAQGE YAGLLAIRGY HQARGEHQRN ICLIPSSAHG
     TNPASAQLAG MDVVVVASDD HGNVDLDDLR AKIEQVGDRL AALMITYPST HGVFEETVTE
     ICERVHAAGG QVYLDGANMN AMVGVAKPGK FGSDVSHLNL HKTFCIPHGG GGPGVGPVAV
     RAHLAPYLPG VLNEQGKLDA EAKVGPVSAA PYGSAGILAI PFVYISLMGA EGLRRATEVA
     ILNANYVATR LREYYPVLYA GRHGRVAHEC ILDIRPLKES IGISAEDIAK RLMDYGFHAP
     TMSFPVAGTL MVEPTESEGL AELERFIDAM IAIRAEVAQV ERGERDREDN VLKNAPHTAQ
     MLLAEEWHHA YPRQQAAYPL ASLRDGKYWP PVARVDNAYG DRNLVCSCLP IEAYI