ID   GCSP_BARQU              Reviewed;         931 AA.
AC   Q6FYZ7;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=BQ10110;
OS   Bartonella quintana (strain Toulouse) (Rochalimaea quintana).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Toulouse;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT   of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897700; CAF26479.1; -; Genomic_DNA.
DR   RefSeq; WP_011179696.1; NC_005955.1.
DR   AlphaFoldDB; Q6FYZ7; -.
DR   SMR; Q6FYZ7; -.
DR   STRING; 283165.BQ10110; -.
DR   EnsemblBacteria; CAF26479; CAF26479; BQ10110.
DR   KEGG; bqu:BQ10110; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_2_1_5; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000000597; 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..931
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000227094"
FT   MOD_RES         684
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   931 AA;  101490 MW;  2A3F818FF424589E CRC64;
     MQERSFFSRH IGLRSDETQK MLDVLGLDCI DTLVSQAIPH SIHLGRVLNL PKAVSEGQAL
     EELSKIMGRN HVHKSFIGQG YHGTCVPPVI LRNLFENPAW YTAYTPYQAE ISQGRLELLF
     YFQTLISELT GLPVAAASLL DEATALAEAN AVAVRFAREK KTKISLQSLL HPQILSVVQT
     RAETQGISIS ENSEICSNTA AIVLSWPDTK GFFNDYSEVI KEAKAKGALV IVVADPLALT
     LMEPPAQWGA DIVVGSMQRY GVPMGFGGPH AGYLAVSDAL IRLIPGRIVG QSVDTKGRVG
     FRLALQTREQ HIRRDKATSN ICTAQALLAN MATAYAVWHG PQGLQEIAQR IHSLTCRFMG
     GLEAAGIPCE GESFFDCVSV VVKGKAQEIA RQAKAGGRLV RILDDDRVAV NFDELSTEED
     ACTLAQLFGA QLVDQVSPRL WGKGRDAAFL SQPFFHVVHS ETDMMRFLRR LSDKDLALDR
     AMIPLGSCTM KLNAAAELMP VSWPTVANIH PFVPKEDAAG YQEMINQLNA WLCEITGFAQ
     VSFQPNSGAQ GEYAGLLAIR RYYQSRGENQ RTLCLVPASA HGTNPASAHM AGMEVVVVKC
     LSDGDVDIDD LKMKAQLHKD RLAALMITYP STHGVYEENI KDICSLIHEN GGQVYFDGAN
     LNALVGLTRP ADIGADVCHM NLHKTFAIPH GGGGPGVGPI GVAEHLKPFL PGHAQNGTTH
     AVSAAPYGSA SILVITWMYI RMMGAKGLKY ATQTAILNAN YIAERLSQAY SILYRGKHGR
     VAHECIVDTR VLKEQYGVSV DDIAKRLIDY GFHAPTMSFP VPGTLMIEPT ESEPKAEIDR
     FCDALLSIAE EAKKVGAGVW PKDDNPLVNA PHTLVDTLDD AWVHPYSRQE AAFPNHHLDP
     TNKYWPPVSR IDNVAGDRVL ICSCPPLGNT S