ID   GCSP_BACFR              Reviewed;         949 AA.
AC   Q64UQ7;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 101.
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=BF2025;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(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=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC         complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC         L-lysyl-[glycine-cleavage complex H protein]; 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; AP006841; BAD48772.1; -; Genomic_DNA.
DR   RefSeq; WP_011202698.1; NC_006347.1.
DR   RefSeq; YP_099306.1; NC_006347.1.
DR   AlphaFoldDB; Q64UQ7; -.
DR   SMR; Q64UQ7; -.
DR   STRING; 295405.BF2025; -.
DR   KEGG; bfr:BF2025; -.
DR   PATRIC; fig|295405.11.peg.1971; -.
DR   HOGENOM; CLU_004620_3_2_10; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000002197; 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR003437; GcvP.
DR   InterPro; IPR049316; GDC-P_C.
DR   InterPro; IPR049315; GDC-P_N.
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   NCBIfam; TIGR00461; gcvP; 1.
DR   PANTHER; PTHR11773:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   Pfam; PF02347; GDC-P; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate.
FT   CHAIN           1..949
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000227091"
FT   MOD_RES         704
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   949 AA;  104679 MW;  8826948720335871 CRC64;
     MKTDLLACRH IGVNKADAEV MLRKIGVASL DELIDKTIPA NIRLKAPLAL PAPMTEYEFA
     RHIAELAGKN KLFTTYIGMG WYNTITPAVI QRNVFENPVW YTSYTPYQTE VSQGRLEALM
     NFQTAVCDLT AMPLANCSLL DEATAAAEAV TMMYGLRSRN QQKAGANVVF IDENIFPQTL
     AVITTRAIPQ DIEIRTGKFR DLEFTDDLFA CVLQYPNANG NAEDYREFTE KAHTANCKVA
     VAADILSLAL LTPPGEWGAD IVFGTTQRLG TPMFYGGPSA GYFATRDEYK RNMPGRIIGW
     SKDKYGKLCY RMALQTREQH IKREKATSNI CTAQALLATM AGFYTVYHGQ EGIRNIASRI
     HSITVFLEKS ISKLGFKQVN 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
//