ID   GCSP_MYCBO              Reviewed;         941 AA.
AC   Q7VET8; A0A1R3XZT5; X2BIL8;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
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}; Synonyms=gcvB;
GN   OrderedLocusNames=BQ2027_MB1863;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIU00467.1; -; Genomic_DNA.
DR   RefSeq; NP_855515.1; NC_002945.3.
DR   RefSeq; WP_010950613.1; NC_002945.4.
DR   AlphaFoldDB; Q7VET8; -.
DR   SMR; Q7VET8; -.
DR   EnsemblBacteria; SIU00467; SIU00467; BQ2027_MB1863.
DR   PATRIC; fig|233413.5.peg.2042; -.
DR   OMA; CVPMSEY; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProt.
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..941
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000166918"
FT   MOD_RES         692
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   941 AA;  99453 MW;  4572D7C6FC2CEA8B CRC64;
     MSDHSTFADR HIGLDSQAVA TMLAVIGVDS LDDLAVKAVP AGILDTLTDT GAAPGLDSLP
     PAASEAEALA ELRALADANT VAVSMIGQGY YDTHTPPVLL RNIIENPAWY TAYTPYQPEI
     SQGRLEALLN FQTLVTDLTG LEIANASMLD EGTAAAEAMT LMHRAARGPV KRVVVDADVF
     TQTAAVLATR AKPLGIEIVT ADLRAGLPDG EFFGAIAQLP GASGRITDWS ALVQQAHDRG
     ALVAVGADLL ALTLIAPPGE IGADVAFGTT QRFGVPMGFG GPHAGYLAVH AKHARQLPGR
     LVGVSVDSDG TPAYRLALQT REQHIRRDKA TSNICTAQVL LAVLAAMYAS YHGAGGLTAI
     ARRVHAHAEA IAGALGDALV HDKYFDTVLA RVPGRADEVL ARAKANGINL WRVDADHVSV
     ACDEATTDTH VAVVLDAFGV AAAAPAHADI ATRTSEFLTH PAFTQYRTET SMMRYLRALA
     DKDIALDRSM IPLGSCTMKL NAAAEMESIT WPEFGRQHPF APASDTAGLR QLVADLQSWL
     VLITGYDAVS LQPNAGSQGE YAGLLAIHEY HASRGEPHRD ICLIPSSAHG TNAASAALAG
     MRVVVVDCHD NGDVDLDDLR AKVGEHAERL SALMITYPST HGVYEHDIAE ICAAVHDAGG
     QVYVDGANLN ALVGLARPGK FGGDVSHLNL HKTFCIPHGG GGPGVGPVAV RAHLAPFLPG
     HPFAPELPKG YPVSSAPYGS ASILPITWAY IRMMGAEGLR AASLTAITSA NYIARRLDEY
     YPVLYTGENG MVAHECILDL RGITKLTGIT VDDVAKRLAD YGFHAPTMSF PVAGTLMVEP
     TESESLAEVD AFCEAMIGIR AEIDKVGAGE WPVDDNPLRG APHTAQCLLA SDWDHPYTRE
     QAAYPLGTAF RPKVWPAVRR IDGAYGDRNL VCSCPPVEAF A