ID   GCSP_SHEHH              Reviewed;         966 AA.
AC   B0TSG5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Shal_3373;
OS   Shewanella halifaxensis (strain HAW-EB4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=458817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL   Submitted (JAN-2008) 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; CP000931; ABZ77919.1; -; Genomic_DNA.
DR   RefSeq; WP_012278439.1; NC_010334.1.
DR   AlphaFoldDB; B0TSG5; -.
DR   SMR; B0TSG5; -.
DR   STRING; 458817.Shal_3373; -.
DR   PRIDE; B0TSG5; -.
DR   EnsemblBacteria; ABZ77919; ABZ77919; Shal_3373.
DR   KEGG; shl:Shal_3373; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_6; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000001317; 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..966
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000083214"
FT   MOD_RES         713
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   966 AA;  105222 MW;  6E472F25B12C8C79 CRC64;
     MTTETLTQLE QHELFIRRHI GPESTQQQEM LNFVGAESLE DLTQQIVPGS IRLNRDLAVG
     SSCSEAEGMA YIREVADKNK VFKSYIGMGY YGTEVPSVIQ RNVFENPGWY TAYTPYQPEI
     AQGRLEAILN FQQVSMDLTG LDLASASLLD EATAAAEAMA LAKRVSKAKK ANIFFIADDV
     FPQTIDVVKT RAECFGFDIV VGPASDAVNY ELFGALFQYT NRFGEISDHT ALFAELKAKK
     AVVTVAADMM SLVLLKSPGS MGADVVFGSA QRFGVPMGFG GPHAAFFVTR DEYKRSLPGR
     IIGVSQDTRG NRALRMAMQT REQHIRREKA NSNICTAQVL LANMASFYAV YHGPQGLKVI
     AERIHRLTDI LAAGLTAKGL ELVNSTWFDT ITVKGGDVAA INARALAAQI NLRIDSANDN
     AGSFGISLDE TTTRTDVSEL FDVILGSEHG LDVAALDEQI IKADSASIPS ELVRTDAILT
     HPTFNRYHSE TEMMRYIKRL ENKDLALNHS MISLGSCTMK LNAATEMMPV SWAEFGNMHP
     FCPLDQAEGY TQLIEELSAW LVDITGYDAM CMQANSGASG EYAGLLAIRN YHISRGEGHR
     NVCLIPQSAH GTNPASAQLA GMKIVVTACD KAGNVDMEDL KTKAAEVADN LSCIMITYPS
     THGVYEETVS EICDIIHQHG GQVYLDGANM NAQVGLTTPG SIGADVSHLN LHKTFAIPHG
     GGGPGMGPIG VKAHLAPFVA GHSVVKPGRE SDNNGAVSAA PYGSASILPI TWMYIKLLGY
     QGLRQSTQVA LLNANYVMKK LSAHYPVLYT GRNDRVAHEC IIDLRPLKEA SGVTEMDIAK
     RLNDYGFHAP TMSFPVAGTL MIEPTESESK VELDRFIEAM VSIRAEIAKV ESGEWPVDNN
     PLHNAPHTLA DIMDPAFDER PYTRQEAVFP TAAVKANKFW PTVNRIDDVY GDRNLMCSCA
     PVSDYE