ID   GCSP_DECAR              Reviewed;         963 AA.
AC   Q47D81;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=Daro_2465;
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC   Dechloromonas.
OX   NCBI_TaxID=159087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCB;
RX   PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA   Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA   Lapidus A.;
RT   "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT   indications of a surprisingly complex life-style and cryptic anaerobic
RT   pathways for aromatic degradation.";
RL   BMC Genomics 10:351-351(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; CP000089; AAZ47200.1; -; Genomic_DNA.
DR   RefSeq; WP_011288199.1; NC_007298.1.
DR   AlphaFoldDB; Q47D81; -.
DR   SMR; Q47D81; -.
DR   STRING; 159087.Daro_2465; -.
DR   PRIDE; Q47D81; -.
DR   EnsemblBacteria; AAZ47200; AAZ47200; Daro_2465.
DR   KEGG; dar:Daro_2465; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_4; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
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; IPR018247; EF_Hand_1_Ca_BS.
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..963
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000227103"
FT   MOD_RES         707
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   963 AA;  104019 MW;  B6FAF847CADABB8A CRC64;
     MPLNLPLSAL EQHDEFIGRH IGPCSTEMAT MLTAIGADSL EQLIDQTVPA AIRLPADLPL
     PAPRREHEAL ADLKAMASKN VVNKSCIGMG YYDTLTPKVI LRNVMENPGW YTAYTPYQAE
     IAQGRLEALM NFQQMVIDLT GLEIANASLL DEATAAAEAM TMARRVSKSK SNRFLVDANC
     FPQSIDVVKT RAAYFGFELV IGNIDAHKDG DFFGALLQYP GDNGEVRDLT DVIAGLKAKG
     TTVAVASDLM ALVLLKSPGA MGADIALGSS QRFGIPMGFG GPHAAFFATR EAFVRSMPGR
     IIGISKDARG NTAYRMALQT REQHIRREKA NSNICTSQVL LANMAGMYVV YHGAEGLRTI
     AGRIHRLTAI LAEGLKRASV NLLTKQFYDT VHFDLGARAE SVYNDALAAG YNLRRVSAGV
     LGISFDETTT RDDVATLFKL IAQTTLDVAT IDAQVAAADS ALPDSLIRSD AVLQHPVFNT
     HHTEHEMLRY LKSLQNKDLA LDHSMISLGS CTMKLNATSE MIPVTWPEFG GIHPFAPRDQ
     AVGYLEMITS LTEWLKTVTG FDAICMQPNS GAQGEYAGLV AIDRFHASRG EEHRNVCLIP
     KSAHGTNPAT AQMANMKVVV VDCDENGNVD VADLKAKAEE HKDDLACLMI TYPSTHGVFE
     EAIRDICAIV HANGGQVYMD GANLNAQVGL TSPGFIGADV SHMNLHKTFA IPHGGGGPGM
     GPIGLKAHLA PFMADHVVQP TGDANRVNAG QGAVSAAPFG SASILTISWM YLAMLGGAGV
     KKATQVAILN ANYVAKQLNA HYPVLYVGKN GRVAHECILD IRPIKAATGI AEIDIAKRLM
     DYGFHAPTVS FPVAGTIMVE PTESESKAEL DRFIGAMIAI REEIRQIENG VWTADNNPLK
     NAPHSQADVM DAEWKHPYSR QQAVFPLPWV AANKFWPSVN RIDDVYGDRN LNCACPPMEA
     YAD