ID   GCSP_MYCA1              Reviewed;         941 AA.
AC   A0QGN2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=MAV_2884;
OS   Mycobacterium avium (strain 104).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=243243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000479; ABK68698.1; -; Genomic_DNA.
DR   RefSeq; WP_011725113.1; NC_008595.1.
DR   AlphaFoldDB; A0QGN2; -.
DR   SMR; A0QGN2; -.
DR   EnsemblBacteria; ABK68698; ABK68698; MAV_2884.
DR   KEGG; mav:MAV_2884; -.
DR   HOGENOM; CLU_004620_3_2_11; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000001574; 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_1000045589"
FT   MOD_RES         692
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   941 AA;  99961 MW;  D8668C4BC2C65BCA CRC64;
     MPDHTTFAAR HIGPDPQAVA AMLDVIGVGS LDELAAKAVP AGIRDRLSAD GIAPGLDRLP
     PPASETEALA ELRGLAEANT VAVSMIGQGY YDTLTPPVLL RNILENPAWY TAYTPYQPEI
     SQGRLEALLN FQTMVADLTG LEIANASMLD EGTAAAEAMT LMHRASRGKS NRLAVDVDVF
     AQTAAIVATR ARPLGIEIVT ADLRDGLPDG DFFGVIAQLP GASGAITDWA ALVAQAHERG
     ALVALGADLL ALTLITPPGE IGADVAFGTT QRFGVPMGFG GPHAGYLAVH ANHARQLPGR
     LVGVSLDADG SPAYRLALQT REQHIRRDKA TSNICTAQVL LAVMAAMYAS YHGAEGLTAI
     ARRVHGHAEA IAAALGTAVV HDRYFDTVLA RVPGRAHEVI AAAKARGINL WRVDDDHVSV
     ACDEATTDEH VAAVLEAFGV APAEPVASEI ATRTSEFLTH PAFTQYRTET AMMRYLRTLA
     DKDIALDRSM IPLGSCTMKL NAAAEMEPIT WPEFARQHPF APASDTPGLR RLIGDLENWL
     VAITGYDAVS LQPNAGSQGE YAGLLAIHDY HASRGEPHRD ICLIPSSAHG TNAASAALAG
     MRVVVVGCHD NGDVDLDDLR AKVTDHRDRL STLMITYPST HGVYEHDIAE ICAAVHDAGG
     QVYVDGANLN ALVGLARPGK FGGDVSHLNL HKTFCIPHGG GGPGVGPVAV RSHLAPFLPG
     HPHAPELPQG HPVSSAPYGS ASILPISWAY IRMMGADGLR AASLTAITSA NYIARRLDEY
     FPVLYTGENG MVAHECILDL RPITKATGVT VDDVAKRLAD YGFHAPTMSF PVAGTLMVEP
     TESETLTEVD AFCDAMIAIR GEIDRVGAGE WPVEDNPLRG APHTAECLVT TDWDHPYSRE
     QAAYPLGKDF RPKVWPPVRR IDGAYGDRNL VCSCPPVEAF A