ID   GCSP_ALIF1              Reviewed;         955 AA.
AC   Q5DZM3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=VF_A0703;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000021; AAW87773.1; -; Genomic_DNA.
DR   RefSeq; WP_011263534.1; NC_006841.2.
DR   RefSeq; YP_206661.1; NC_006841.2.
DR   AlphaFoldDB; Q5DZM3; -.
DR   SMR; Q5DZM3; -.
DR   STRING; 312309.VF_A0703; -.
DR   EnsemblBacteria; AAW87773; AAW87773; VF_A0703.
DR   KEGG; vfi:VF_A0703; -.
DR   PATRIC; fig|312309.11.peg.3305; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_2_1_6; -.
DR   OMA; DEHCHPQ; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000000537; 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; 3.40.640.10; -; 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; Reference proteome.
FT   CHAIN           1..955
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045624"
FT   MOD_RES         705
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   955 AA;  104827 MW;  E15ED1B6CDEA05BD CRC64;
     MSQLLQQLGT DNEFIRRHNG PASSEHQHML NTIGAETLQQ LIEETVPSSI RLPQPMQLPH
     GLSENAMLAE LKQIAQQNTL NTSYIGQGYY NTHTPNVILR NVLENPGWYT AYTPYQPEIS
     QGRLEALLNY QQMVMDLTGL EIANASLLDE ATAAAEAMTL CKRGGKSKSN LFFVADDVHP
     QTLAVIKTRA KFIGFDVVVD HESNLDSHDV FGALLQYPGT TGEVKDLTDL IAQAHTKKTL
     VIVATDLLAS 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 GMDYAVSAAD LGSASILPIS WAYIAMMGEM GLTEATKVAI
     LNANYVMERL RPHYPVLYRG TNGRIAHECI IDIRPLKETT GISEEDIAKR LMDFGFHAPT
     MSFPVAGTLM VEPTESEDLA ELDRFCDAMI AIREEMNKVE QGEWPLDNNP LVNAPHTQVD
     LMSDSWEHPY TREVACFPSS QSKDSKYWPT VNRVDNVYGD RNLICSCPSI ENYEE