ID   GCSP_ALIFM              Reviewed;         955 AA.
AC   B5EUH1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
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};
GN   OrderedLocusNames=VFMJ11_A0790;
OS   Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=388396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11;
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-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=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC         complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC         L-lysyl-[glycine-cleavage complex H protein]; 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; CP001133; ACH64611.1; -; Genomic_DNA.
DR   RefSeq; WP_012535657.1; NC_011186.1.
DR   AlphaFoldDB; B5EUH1; -.
DR   SMR; B5EUH1; -.
DR   GeneID; 77250538; -.
DR   KEGG; vfm:VFMJ11_A0790; -.
DR   HOGENOM; CLU_004620_2_1_6; -.
DR   Proteomes; UP000001857; Chromosome II.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR003437; GcvP.
DR   InterPro; IPR049316; GDC-P_C.
DR   InterPro; IPR049315; GDC-P_N.
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   NCBIfam; TIGR00461; gcvP; 1.
DR   PANTHER; PTHR11773:SF13; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   Pfam; PF02347; GDC-P; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate.
FT   CHAIN           1..955
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000132461"
FT   MOD_RES         705
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   955 AA;  104739 MW;  06414DBC44925621 CRC64;
     MSQLLQQLGT DNEFIRRHNG PASSEHQHML NTIGAETLQQ LIEETVPSSI RLPQPMQLPH
     GLSENAMLAE LKQIAQQNTL NTSYIGQGYY NTHTPNVILR NVLENPGWYT AYTPYQPEIS
     QGRLEALLNY QQMVMDLTGL EIANASLLDE ATAAAEAMTL CKRGGKSKSN IFFVADDVHP
     QTLAVIKTRA KFIGFDVIVD NESNLDSHDV FGALLQYPGT TGEVKDLTDL IAQAHTKKTL
     VVVATDLLAS VLLKPVGEMG ADIAIGSAQR FGVPMGYGGP HAAFMATREK LKRSMPGRVI
     GVSIDSKGNQ ALRMAMQTRE QHIRREKATS NICTAQALLA NMASFYAVYH GPEGLKTIAR
     RVHHFTAIVA KALQTAGFEL EHQHFFDTLT VKTEQQTDIL YTKALASSIN LRKFDTKLGI
     SFDETTTVSD LVTLLAVFGI DNAECETLSA EVGKDEFAAI PKHCQRTSSF LTHPVFNTYH
     SETQMLRYLK KLENKDFSLT HGMIPLGSCT MKLNAVAEML PVTWPEFGGI HPFAPLNQAA
     GYTTLATSLK SMLCEITGYD EFSLQPNSGA SGEYAGLIAI QRYHESRGDA HRNVCLIPSS
     AHGTNPATAS MVSMKVVVVK CDENGNIDMI DLAEKIEKHQ ENLSSIMITY PSTHGVYEEQ
     VREVCDMVHA AGGQVYLDGA NMNAQVGLTS PGFIGSDVSH LNLHKTFCIP HGGGGPGMGP
     IGVKSHLAPF LPGHTENGVQ GTDYAVSAAD LGSASILPIS WAYIAMMGEM GLTEATKVAI
     LNANYVMERL RPHYPVLYRG SNGRIAHECI IDIRPLKEAT GISEEDIAKR LMDFGFHAPT
     MSFPVAGTLM VEPTESEDLA ELDRFCDAMI AIREEMHKVE QGEWPLDNNP LVNAPHTQVD
     LMSDSWDHPY TREVACFPSS QSKDSKYWPT VNRVDNVYGD RNLICSCPSI ENYEE
//