ID   GCSP_BORPD              Reviewed;         957 AA.
AC   A9I7K9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=Bpet4074;
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448;
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
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; AM902716; CAP44422.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9I7K9; -.
DR   SMR; A9I7K9; -.
DR   STRING; 94624.Bpet4074; -.
DR   EnsemblBacteria; CAP44422; CAP44422; Bpet4074.
DR   KEGG; bpt:Bpet4074; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   OMA; CVPMSEY; -.
DR   Proteomes; UP000001225; 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..957
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000190205"
FT   MOD_RES         704
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   957 AA;  102252 MW;  F49F609876EE9BEF CRC64;
     MSRALDPHTD FIPRHIGPTA ADQEKMLAAI GCGSLDALLQ EVVPPAIRSQ GPLALPASRS
     ESDVLADLKA VAGRNRIYRN YIGQGYYGTH TPNVVLRNVL ENPAWYTAYT PYQPEISQGR
     LEALLNYQTM VADLTGLDIS NASLLDEGTA AAEAMTLARR GSKSASQVFF VSAHCHPQTI
     EVVRTRAEGL GIEVALGDEA QGLPECFGVL LQYPHSLGGV ADYRALAEAA HAQGAVVACA
     TDLLALALMT PPGEWGADIA IGSSQRFGVP FGFGGPHAGF MACKDAYKRN MPGRLVGVSK
     DAQGNPALRL ALQTREQHIR REKATSNICT AQVLLAVMAG LYAVWHGPDG IRRIATRVHR
     YTAILRAALT QLGIKVVNDT FFDTLLLETG VATPAIVEAA VCEHINLRRV DGARLAVSLD
     ETVTAADLQA LVNVFAAGLQ KDDLALDIDA HDAAAPGGIP AALQRQGGIL AHPVFSSIQS
     ETDMLRYLRK LADKDLALDR SMIPLGSCTM KLNATAEMIP ITWPEFALIH PYAPADQSAG
     YRELIERLSK ALCEITGYDD ISLQPNSGAQ GEYAGLLAIR GYHRANGQAQ RNVCLIPASA
     HGTNPASAQL AGMEVVVVAS DANGNVDLDD LRAKLTQVGD RLAALMITYP STHGVFEESI
     THICDLVHQA GGQVYLDGAN MNAMVGVARP GKFGSDVSHL NLHKTFCIPH GGGGPGVGPV
     AVRSHLAPFL PGVLNAQGKL GGETGIGPVA AAPYGSAGIL PISYAYIALM GADGLRRATE
     VAILNANYVA ARLRDYYPVL YAGRNGRVAH ECILDVRPLK DSSGISAEDI AKRLMDYGFH
     APTMSFPVAG TLMVEPTESE GLAELERFID AMIAIREEIA QVERGERDRD DNVLKNAPHT
     AQMLLAEEWL HDYPRQQAAY PVASLRDAKY WPPVARVDNA YGDRNLVCAC LPVEAYA