ID   GCSP_BACTN              Reviewed;         949 AA.
AC   Q8A8M0;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=BT_1147;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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; AE015928; AAO76254.1; -; Genomic_DNA.
DR   RefSeq; NP_810060.1; NC_004663.1.
DR   RefSeq; WP_008765866.1; NC_004663.1.
DR   AlphaFoldDB; Q8A8M0; -.
DR   SMR; Q8A8M0; -.
DR   STRING; 226186.BT_1147; -.
DR   PaxDb; Q8A8M0; -.
DR   PRIDE; Q8A8M0; -.
DR   EnsemblBacteria; AAO76254; AAO76254; BT_1147.
DR   GeneID; 60927124; -.
DR   KEGG; bth:BT_1147; -.
DR   PATRIC; fig|226186.12.peg.1169; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_10; -.
DR   InParanoid; Q8A8M0; -.
DR   OMA; CVPMSEY; -.
DR   Proteomes; UP000001414; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central.
DR   GO; GO:0016594; F:glycine binding; IBA:GO_Central.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
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_0000166903"
FT   MOD_RES         704
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   949 AA;  104967 MW;  90222CFA46E06AE6 CRC64;
     MKTDLLASRH IGINEEDTAV MLRKIGVDSL DELINKTIPA NIRLKEPLAL AKPLTEYEFG
     KHIADLASKN KLYTTYIGLG WYNTITPAVI QRNVFENPVW YTSYTPYQTE VSQGRLEALM
     NFQTAVCDLT AMPLANCSLL DEATAAAEAV TMMYALRSRT QQKAGANVVF VDENIFPQTL
     AVMTTRAIPQ GIELRVGKYK EFEPSPEIFA CILQYPNSSG NVEDYADFTK KAHEADCKVA
     VAADILSLAL LTPPGEWGAD IVFGTTQRLG TPMFYGGPSA GYFATRDEYK RNMPGRIIGW
     SKDKYGKLCY RMALQTREQH IKREKATSNI CTAQALLATM AGFYAVYHGQ EGIKTIASRI
     HSITVFLDKQ LKKFGYTQVN AQYFDTLRFE LPEHVSAQQI RTIALSKEVN LRYYENGDVG
     FSIDETTDIA ATNVLLSIFA IAAGKDYQKV EDVPEKSNID KALKRTTPFL THEVFSNYHT
     ETEMMRYIKR LDRKDISLAQ SMISLGSCTM KLNAAAEMLP LSRPEFMSMH PLVPEDQAEG
     YRELISNLSE DLKVITGFAG VSLQPNSGAA GEYAGLRVIR AYLESIGQGH RNKILIPASA
     HGTNPASAIQ AGFETVTCAC DEQGNVDMGD LRAKAEENKE ALAALMITYP STHGIFETEI
     KEICEIIHAC GAQVYMDGAN MNAQVGLTNP GFIGADVCHL NLHKTFASPH GGGGPGVGPI
     CVAEHLVPFL PGHSIFGSTQ NQVSAAPFGS AGILPITYGY IRMMGTEGLT QATKIAILNA
     NYLAACLKDT YGIVYRGATG FVGHEMILEC RKVHEETGIS ENDIAKRLMD YGYHAPTLSF
     PVHGTLMIEP TESESLAELD NFVDVMLNIW KEIQEVKNEE ADKNDNVLIN APHPEYEIVN
     DNWEHSYTRE KAAYPIESVR ENKFWVNVAR VDNTLGDRKL LPTRYGTFE