ID   GCSP_SHEFN              Reviewed;         962 AA.
AC   Q07YC9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   25-MAY-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=Sfri_3149;
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA   Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-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; CP000447; ABI72985.1; -; Genomic_DNA.
DR   RefSeq; WP_011638588.1; NC_008345.1.
DR   AlphaFoldDB; Q07YC9; -.
DR   SMR; Q07YC9; -.
DR   STRING; 318167.Sfri_3149; -.
DR   EnsemblBacteria; ABI72985; ABI72985; Sfri_3149.
DR   KEGG; sfr:Sfri_3149; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000000684; 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; -; 1.
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; Reference proteome.
FT   CHAIN           1..962
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045609"
FT   MOD_RES         709
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   962 AA;  104802 MW;  1CCDF7FAC46FE711 CRC64;
     MTKQTLTQLE QHELFLTRHI GPNAEQQQEM LNFIGAESLE DLTAQTVPGK IRLPQDLTIG
     DSCGEAEGIA YIRNIADKNK VFKSYIGMGY YGVQVPNVIL RNVFENPGWY TAYTPYQPEI
     AQGRLEAILN FQQVSMDLTG LDLASASLLD EATAAAEAMA LAKRVSKAKK ANIFFVADDV
     FPQTLDVVKT RAECFGFEVV VGPASEAVNY ELFGALFQYT NRIGQITDYT ELFATLRDNK
     VIVTVAADIM SLMLLKSPGA MGADVVFGSA QRFGVPMGYG GPHAAFFVAR DEHKRSMPGR
     IIGVSKDTRG NSALRMAMQT REQHIRREKA NSNICTAQIL LANMASFYAV FHGPQGLKTI
     ASRINRLADI LAAGLTAKGL TLANTTWFDT ISVKGADVAA INARAIAAQV NLRIDADGVF
     GISLDETTIR TDIADLFDVI LGAGHGLDVA TFDADIVANG SQSIPDALVR QDAVLTHPTF
     NRYQSETEMM RYIKRLENKD LALNHSMISL GSCTMKLNAA VEMLPVSWPE FANMHPFCPL
     DQAQGYTQLI NELSEFLVKI TGYDSVCIQP NSGAQGEYAG LLAIKKYHES RGDAHRNICL
     IPQSAHGTNP ASAQLAGMKV VVTACDKQGN VDLEDLRTKA AELADSLSCI MITYPSTHGV
     YEESIREVCE IVHQYGGQVY LDGANMNAQV GLTSPGFIGA DVSHLNLHKT FAIPHGGGGP
     GMGPIGVKSH LAPFVAGHTV IKPGRESDHN GAVSAAPYGS ASILPISWMY IKLLGTKGVK
     QSTQTALLNA NYIMKKLSAH YPVLFTGRND RVAHECIIDL RPLKETSGVT EMDIAKRLND
     YGFHSPTMSF PVAGTLMIEP TESESKVELD RFIEAMISIR GEITKVEAGE WPVDNNPLHN
     APHTLADIMD PEFDSRPYSR EVAVFPTAAV KANKFWPTVN RIDDVYGDRN LMCSCVPLSD
     YE