ID   GCSP_ALISL              Reviewed;         955 AA.
AC   B6ES35;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=VSAL_II0765;
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=316275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238;
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA   Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA   Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT   LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FM178380; CAQ81519.1; -; Genomic_DNA.
DR   RefSeq; WP_012552059.1; NC_011313.1.
DR   AlphaFoldDB; B6ES35; -.
DR   SMR; B6ES35; -.
DR   STRING; 316275.VSAL_II0765; -.
DR   EnsemblBacteria; CAQ81519; CAQ81519; VSAL_II0765.
DR   KEGG; vsa:VSAL_II0765; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   OMA; TIDICMT; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000001730; Chromosome 2.
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..955
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000190204"
FT   MOD_RES         705
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   955 AA;  104486 MW;  E786273F296B032A CRC64;
     MSQLLQQLGT DNEFIRRHNG PASSQHQHML NTVGAETLEK LIEETVPSSI RLPQPMQLPH
     GLSENAMLAE LKQIAQQNTL NTSYIGQGYY NTHTPNVILR NVFENPGWYT AYTPYQPEIS
     QGRLEALLNY QQMVMDLTGL DIANASLLDE ATAAAEAMTL CKRGGKNKSS TFFVADDVHP
     QTLAVIKTRA KFIGFDVVVD TDSNLDSHDV FGALLQYPGT TGEVKDLTTL IEQAHAKKTL
     VVVATDLLAS VLLKPVGEMG ADIAIGSAQR FGVPMGYGGP HAAFMATREK LKRSMPGRVI
     GVSIDSKGNQ ALRMAMQTRE QHIRREKATS NICTAQALLA NMASFYAVYH GPEGLKTIAR
     RVHHFTAIVA KSLQSAGFEL AHQHFFDTLT VKTEQQTDIL YTKALAASIN LRKFDTELGI
     SFDETTTVSD LVALLAVFGV DNAECDSLSN DIGQDEFAAI PEACRRTSSF LTHPVFNTHH
     SETQMLRYLK KLENKDFSLT HGMIPLGSCT MKLNAVAEML PVTWPEFGGI HPFAPLNQAA
     GYTTLATSLK SMLCEITGYD DFSLQPNSGA SGEYAGLIAI QRYHESRNEG HRNVCLIPSS
     AHGTNPATAS MVSMKVVVVK CDDNGNIDMI DLAEKIAKHQ ENLSSIMITY PSTHGVYEEQ
     VREVCDMVHD AGGQVYLDGA NMNAQVGLTS PGFIGSDVSH LNLHKTFCIP HGGGGPGMGP
     IGVKSHLAPF LPGHSENGVQ GSDYAVSAAD LGSASILPIS WAYIAMMGEM GLTEATKVAI
     LNANYVMDRL RPHYPVLYRG TNGRIAHECI IDIRPLKEAT GISEEDIAKR LMDFGFHAPT
     MSFPVAGTLM IEPTESEDLA ELDRFCEAMI AIREEMNKVQ QGEWPLDNNP LVNAPHTQVD
     LMSNEWDHPY TREVACFPSV QAKASKYWPT VNRVDNVYGD RNLICSCPSI DSYEE