ID   GCSP_BORBR              Reviewed;         954 AA.
AC   Q7WP29;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=BB0856;
OS   Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS   (Alcaligenes bronchisepticus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
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; BX640439; CAE31355.1; -; Genomic_DNA.
DR   RefSeq; WP_010925964.1; NC_002927.3.
DR   AlphaFoldDB; Q7WP29; -.
DR   SMR; Q7WP29; -.
DR   STRING; 257310.BB0856; -.
DR   EnsemblBacteria; CAE31355; CAE31355; BB0856.
DR   KEGG; bbr:BB0856; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_4; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000001027; 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.
FT   CHAIN           1..954
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000166904"
FT   MOD_RES         701
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   954 AA;  102137 MW;  2F08D4F14716B0D6 CRC64;
     MSRAPDTHSD FIPRHIGPSD EDQATMLAAI GAASLDALID EVVPPRIRSR APLALPAARS
     ETDVLQDLKR MAARNQIYRN YIGQGYYGTH TPNVVLRNVL ENPAWYTAYT PYQPEISQGR
     LEALLNYQTM VADLTGLDIS NASLLDEGTA AAEAMTLARR GSRSSSPVFF VSQHCHPQTL
     EVVRTRAEGL GIELVIGDES RGLPECFGVL LQYPHSLGGV ADYRELAQAA HAQGAVVACV
     TDLLALALIE PPGQWGADIA VGSAQRFGVP FGFGGPHAGF MSCRDAYKRN MPGRLVGVSK
     DAQGNPALRL ALQTREQHIR REKATSNICT AQVLLAVMAG LYAVWHGPRG VRRIAERVQS
     LTGALRAALA GLGVKVANDT WFDTLLLETG VATPAILAAA DCARINLRQV DGARLAVSLD
     ETVTLADLQA LVNVFAAGLG KDEVALPAPQ ASLDGIPAAV RRQGPILSHP VFSSVQSETD
     MLRYLRKLAD KDLALDRTMI PLGSCTMKLN ATAEMIPITW PEFALIHPFA PASQTPGYRE
     LIDGLSAQLC EITGYDGISL QPNSGAQGEY AGLLAIRAYH QANGQPQRNV CLIPASAHGT
     NPASAQLAGM DVVVVASDAN GNVDLADLRA RIAQVGERLA ALMITYPSTH GVFEEAVTEI
     CDAVHEAGGQ VYLDGANMNA MVGVAQPGKF GSDVSHLNLH KTFCIPHGGG GPGVGPVAVR
     AHLAPYLPGV LDAQGRLDPE AKVGPVSAAP YGSAGILPIP YVYIALMGAE GLRRATEVAI
     LNANYIAARL RDHYPVLYAG RNGRVAHECI LDVRPLKETS GISAEDIAKR LMDYGFHAPT
     MSFPVAGTLM VEPTESEGLA ELERFIEAMI AIRAEIAQIE SGERDRDDNV LRNAPHTAQM
     LLAEEWHHDY PRQQAAYPVA SLRENKYWPP VARVDNAYGD RNLVCACLPV EAYA