ID   GCSP_FLAJ1              Reviewed;         949 AA.
AC   A5FMT0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=Fjoh_0445;
OS   Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS   14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=376686;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101;
RX   PubMed=19717629; DOI=10.1128/aem.01495-09;
RA   McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA   Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA   Cheng Y.Q., Stein J.L.;
RT   "Novel features of the polysaccharide-digesting gliding bacterium
RT   Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL   Appl. Environ. Microbiol. 75:6864-6875(2009).
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; CP000685; ABQ03481.1; -; Genomic_DNA.
DR   RefSeq; WP_012022537.1; NZ_MUGZ01000005.1.
DR   AlphaFoldDB; A5FMT0; -.
DR   SMR; A5FMT0; -.
DR   STRING; 376686.Fjoh_0445; -.
DR   EnsemblBacteria; ABQ03481; ABQ03481; Fjoh_0445.
DR   KEGG; fjo:Fjoh_0445; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_10; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000006694; 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; 3.40.640.10; -; 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..949
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000083207"
FT   MOD_RES         700
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   949 AA;  103684 MW;  8CE513D8C3C2F7E9 CRC64;
     MKTDAFALRH IGPRETDLQH MLQTIGVDSI EQLVYETLPD DIRLKAPLNL DPAMTEYEFA
     NHIQELGKKN KVFKSYIGLG YHPTIVPAPI QRNIFENPGW YTAYTPYQAE IAQGRLEAIL
     NFQTTVIELT GMEIANASLL DEGTAAAEAM ALLFDVRTRD QKKNNTHKFF VSEEILPQTL
     SVLQTRSTPI GIELVVGNHE TFDFSTEFFG AILQYPGKYG QVNDYGAFVA KAKENEIKVA
     FAADILSLAA LTSPGEMGAA VVVGTTQRFG VPMGYGGPHA AYFATKDEYK RSMPGRIIGV
     SVDANGNRAL RMALGTREQH IKREKATSNI CTAQVLLAVM AGMYAVYHGP KGLKYIANKV
     HASAVTTAEA LNKLGVFQTN TAFFDTILVK ADAQKVKAIA EKNEVNFFYP DAESVSISLN
     ETTSVSDINQ IIAIFAEALG KEAVTVSELT TASQLPASLE RTSSFLTHDV FNNHHSESQL
     MRYIKKLERK DLSLNHSMIS LGSCTMKLNA ASEMLPLSMP NWNSIHPFAP VEQAEGYITM
     LKKLEQQLNV ITGFAGTTLQ PNSGAQGEYA GLMAIRAYHL SRNEGHRNVC LIPSSAHGTN
     PASAAMAGMK IIVTKTTPEG NIDVEDLREK AIEHKDDLSC LMVTYPSTHG VFESSIIEIT
     KLIHENGGLV YMDGANMNAQ VGLTNPATIG ADVCHLNLHK TFAIPHGGGG PGVGPICVNE
     KLVPFLPTNP ILKVGGEQAI TAISSAPYGS ALVCLISYGY ITMMGAEGLK SATEHAILNA
     NYMKSRFEGH YPILYTGECG RAAHEMILDC RAFKENGIEV GDIAKRLMDY GFHAPTVSFP
     VAGTLMIEPT ESEDLAELDR FCDALISIRK EIEAATADDK NNVLKNAPHT LAMLTSDSWD
     FPYSREKAAY PLEYIADNKF WPSVRRVDDA YGDRNLVCSC APIEAYMEN