ID   GCSP_BORPE              Reviewed;         954 AA.
AC   Q7W0E3;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 95.
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=BP0197;
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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; BX640411; CAE40576.1; -; Genomic_DNA.
DR   RefSeq; NP_879086.1; NC_002929.2.
DR   RefSeq; WP_010929677.1; NZ_CP039022.1.
DR   AlphaFoldDB; Q7W0E3; -.
DR   SMR; Q7W0E3; -.
DR   STRING; 257313.BP0197; -.
DR   KEGG; bpe:BP0197; -.
DR   PATRIC; fig|257313.5.peg.209; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_4; -.
DR   OMA; CVPMSEY; -.
DR   Proteomes; UP000002676; 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..954
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000166906"
FT   MOD_RES         701
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   954 AA;  102077 MW;  2DCD14ECA567D5BD CRC64;
     MSRAPDTHSD FIPRHIGPSD EDQATMLVAI GAASLDALID EVVPPRIRSR APLALPAARS
     ETDVLQDLKR IAARNQIYRN YIGQGYYGTH TPNVVLRNVL ENPAWYTAYT PYQPEISQGR
     LEALLNYQTM VADLTGLDIS NASLLDEGTA AAEAMTLARR GSRSSSPVFF VSQHCHPQTL
     EVVRTRAEGL GIELVIGDES RGLPECFGVL LQYPHSLGGV ADYRELAQAA HAQGAVVACV
     TDLLALALIE PPGQWGADIA VGSAQRFGVP FGFGGPHAGF MACRDAYKRN MPGRLVGVSK
     DAQGNPALRL ALQTREQHIR REKATSNICT AQVLLAVMAG LYAVWHGPRG VRRIAERVQS
     LTGALRAALA GLGVKVANDT WFDTLSLETG AATPAILAAA DCARINLRQV DGARLAVSLD
     ETVTLADLQA LVNVFAAGLG KDEVALAPPQ ASLDGIPAAV RRQGPILSHP VFSSVQSETD
     MLRYLRKLAD KDLALDRTMI PLGSCTMKLN ATAEMIPITW PEFALIHPFA PASQTPGYRE
     LIEGLSAQLC EITGYDGISL QPNSGAQGEY AGLLAIRAYH QANGQPQRNV CLIPASAHGT
     NPASAQLAGM DVVVVASDAN GNVDLADLRA RIAQVGERLA ALMITYPSTH GVFEEAVTEI
     CDAVHEAGGQ VYLDGANMNA MVGVAQPGKF GSDVSHLNLH KTFCIPHGGG GPGVGPVAVR
     AHLAPYLPGV LDARGRLDPE AKVGPVSAAP YGSAGILPIP YVYIALMGAE GLRRATEVAI
     LNANYIATRL RGHYPVLYAG RNGRVAHECI LDVRPLKETS GISAEDIAKR LMDYGFHAPT
     MSFPVAGTLM VEPTESEGLA ELERFIEAMI AIRAEIAQVE SGERDRDDNV LRNAPHTAQM
     LLAEEWHHDY PRQQAAYPVA SLRENKYWPP VARVDNAYGD RNLVCACLPV EAYA