ID   GCSP_MYCPA              Reviewed;         941 AA.
AC   Q73ZQ6;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 112.
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};
GN   OrderedLocusNames=MAP_1545;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(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=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; AE016958; AAS03862.1; -; Genomic_DNA.
DR   RefSeq; WP_010949258.1; NZ_CP106873.1.
DR   AlphaFoldDB; Q73ZQ6; -.
DR   SMR; Q73ZQ6; -.
DR   STRING; 262316.MAP_1545; -.
DR   KEGG; mpa:MAP_1545; -.
DR   PATRIC; fig|262316.17.peg.1636; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_11; -.
DR   Proteomes; UP000000580; 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; Reference proteome.
FT   CHAIN           1..941
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000227107"
FT   MOD_RES         692
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   941 AA;  99928 MW;  70BFCDC8948B1BF3 CRC64;
     MPDHTTFAAR HIGPDPQAVA AMLDVIGVGS LDELAAKAVP AGIRDRLSAD GIAPGLDRLP
     PPASETEALA ELRGLAEANT VAVSMIGQGY YDTLTPPVLL RNILENPAWY TAYTPYQPEI
     SQGRLEALLN FQTMVADLTG LEIANASMLD EGTAAAEAMT LMRRASRGKS NRLAVDADVF
     AQTAAIVATR ARPLGIEIVT ADLRDGLPDG DFFGVIAQLP GASGAITDWA ALVAQAHERG
     ALVALGADLL ALTLITPPGE IGADVAFGTT QRFGVPMGFG GPHAGYLAVH ANHARQLPGR
     LVGVSLDADG SPAYRLALQT REQHIRRDKA TSNICTAQVL LAVMAAMYAS YHGAEGLTAI
     ARRVHGHAEA IAAALGTAVV HDRYFDTVLA RVPGRADEVI AAAKARGINL WRVDDDHVSV
     ACDEATTDEH VAAVLEAFGV APAEPVASEI ATRTAEFLTH PAFTQYRTET AMMRYLRTLA
     DKDIALDRSM IPLGSCTMKL NAAAEMEPIT WPEFARQHPF APASDTPGLR RLIGDLENWL
     VAITGYDAVS LQPNAGSQGE YAGLLAIHDY HASRGEPHRD ICLIPSSAHG TNAASAALAG
     MRVVVVGCHD NGDVDLDDLR AKVTEHRDRL 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
//