ID   GCSP_BARHE              Reviewed;         931 AA.
AC   Q6G2F1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=BH12820;
OS   Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS   (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
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; BX897699; CAF28056.1; -; Genomic_DNA.
DR   RefSeq; WP_011181096.1; NZ_LRIJ02000001.1.
DR   AlphaFoldDB; Q6G2F1; -.
DR   SMR; Q6G2F1; -.
DR   STRING; 283166.BH12820; -.
DR   PaxDb; Q6G2F1; -.
DR   PRIDE; Q6G2F1; -.
DR   EnsemblBacteria; CAF28056; CAF28056; BH12820.
DR   KEGG; bhe:BH12820; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   OMA; CVPMSEY; -.
DR   Proteomes; UP000000421; 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_0000227093"
FT   MOD_RES         684
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   931 AA;  101973 MW;  AE803D14096288F7 CRC64;
     MLERPFFSRH IGLRPDEKQK MLDIVAVDSI DTLVSQALPH SIHLGRPLNL PKAVSEGQAL
     EELSKMMERN YLHKSFIGQG YHGTYVPPVI LRNLFENPAW YTAYTPYQAE ISQGRLELLF
     YFQTLISELT GLPVAAASLL DEATALAEAI TVAFRFTREK KMKISLQSLL HPQILSVVQT
     RAETQGLQVS KNSEICSDTA AIVLSWPDTK GSFNDYSEVI KEAKAKGALV IVVADPLALT
     LMEAPAKWGA DIVVGSMQRY GVPMGFGGPH AGYLAVSDAL TRLIPGRIVG QSVDTKGRVG
     FRLALQTREQ HIRRDKATSN ICTAQALLAN MATAYAVWHG PQGLQEIAQR VHHLTCRFVG
     GLEAVGISCE GEYFFDCVSI VVKGKAREIA CQAKAGGRLI RVLDDDRVVI NFDELSTQED
     AHALAQLFGA GLVDQASPRL MGKGRDTTFL SQPFFHAVHS ETDMMRFLRR LSDKDLALDR
     AMIPLGSCTM KLNAAAELMP VSWPTVANIH PFASREDAVG YQEMIHQLNA WLCEITGFAQ
     VSFQPNSGAQ GEYAGLLAIR RYHQSRGEHQ RTLCLIPASA HGTNPASAHM AGMEVVVVKC
     LNDGDVDLDD LKMKAQLYKE RLAALMITYP STHGVYEESI KDICSLIHEN GGQVYFDGAN
     LNALVGLARP ADIGADVCHM NLHKTFAIPH GGGGPGVGPI GVVEHLKPFL PGHEQEGTTH
     AVSAAPYGSA SILVITWMYI RMMGAEGLKY ATQTAILNAN YIAARLSQVY SILYRGKHGR
     VAHECIVDTR VLKEQYGVSV DDIAKRLIDY GFHAPTMSFP VPGTLMIEPT ESEPKAEIDR
     FCDALLSIAE EAKKIGSGVW PKDDNPLVHA PHTLVDTLDD TWARPYSRQE AAFPNCSLDP
     ANKYWPPVSR IDNVAGDRML ICSCPPLGNT Y