ID   GCSP_BACFN              Reviewed;         949 AA.
AC   Q5LDN2;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=BF2079;
OS   Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS   / NCTC 9343 / Onslow).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=272559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX   PubMed=15746427; DOI=10.1126/science.1107008;
RA   Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA   Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA   Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA   Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA   Barrell B.G., Parkhill J.;
RT   "Extensive DNA inversions in the B. fragilis genome control variable gene
RT   expression.";
RL   Science 307:1463-1465(2005).
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; CR626927; CAH07776.1; -; Genomic_DNA.
DR   RefSeq; WP_005800134.1; NC_003228.3.
DR   AlphaFoldDB; Q5LDN2; -.
DR   SMR; Q5LDN2; -.
DR   STRING; 272559.BF9343_1995; -.
DR   EnsemblBacteria; CAH07776; CAH07776; BF9343_1995.
DR   KEGG; bfs:BF9343_1995; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_10; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000006731; 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..949
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000227092"
FT   MOD_RES         704
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   949 AA;  104591 MW;  DFCC4995CFFE151D CRC64;
     MKTDLLACRH IGVNKADAEV MLRKIGVASL DELIDKTIPA NIRLKAPLAL PAPMTEYEFA
     RHIAELAGKN KLFTTYIGMG WYNTITPAVI QRNVFENPVW YTSYTPYQTE VSQGRLEALM
     NFQTAVCDLT AMPLANCSLL DEATAAAEAV TMMYGLRSRN QQKAGANVVF IDENIFPQTL
     AVITTRAIPQ GIEIRTGKFR DLEFTDDLFA CVLQYPNANG NAEDYREFTE KAHTANCKVA
     VAADILSLAL LTPPGEWGAD IVFGTTQRLG TPMFYGGPSA GYFATRDEYK RNMPGRIIGW
     SKDKYGKLCY RMALQTREQH IKREKATSNI CTAQALLATM AGFYTVYHGQ EGIRNIASRI
     HSITVFLEKS IGKLGFKQVN KQYFDTLRFI LPDSVSAQQI RTIALSKEVN LRYFDNGDVG
     LSIDETTDVA AANILLSIFA IAAGKDFQKV DDIPEATIIS EELKRQTPYL THEVFSKYHT
     ETEMMRYIKR LDRKDISLAQ SMISLGSCTM KLNAAAEMLP LSCAEFMCMH PLVPEDQAAG
     YRELIHNLSE ELKVITGFAG VSLQPNSGAA GEYAGLRTIR AYLESIGQGH RNKVLIPASA
     HGTNPASAIQ AGFTTVTCAC DEHGNVDMDD LRAKAEENKD DLAALMITYP STHGIFETEI
     VEICQIIHAC GAQVYMDGAN MNAQVGLTNP GFIGADVCHL NLHKTFASPH GGGGPGVGPI
     CVAEHLVPFL PGHGLFGNSQ NEVSAAPFGS AGILPITYGY IRMMGAEGLT MATKTAILNA
     NYLAACLKDT YGIVYRGANG FVGHEMILEC RKVYEETGIS ENDIAKRLMD YGYHAPTLSF
     PVHGTLMIEP TESESLSELD NFVLTMLTIW NEIQEVKNGE ADKEDNVLIN APHPEYEVVS
     DQWEHCYTRE KAAYPIESVR ENKFWVNVAR VDNTLGDRKL LPTCYGCFD