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GCSP_XANC5
ID   GCSP_XANC5              Reviewed;         954 AA.
AC   Q3BW89;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 97.
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=XCV1243;
OS   Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=316273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=85-10;
RX   PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005;
RA   Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA   Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA   Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA   Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S.,
RA   Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA   Kaiser O.;
RT   "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT   Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT   genome sequence.";
RL   J. Bacteriol. 187:7254-7266(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; AM039952; CAJ22874.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3BW89; -.
DR   SMR; Q3BW89; -.
DR   STRING; 456327.BJD11_16410; -.
DR   EnsemblBacteria; CAJ22874; CAJ22874; XCV1243.
DR   KEGG; xcv:XCV1243; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_6; -.
DR   OMA; CVPMSEY; -.
DR   Proteomes; UP000007069; 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..954
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045626"
FT   MOD_RES         702
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   954 AA;  102578 MW;  17303C000C2FAECC CRC64;
     MSQTPSSLRD LEHHSAFVER HIGPNDAEIA QMLDVVGHAC LDALTDAIVP GNIKSPAPLA
     LPEAITEEEA LAKIRAIADK NTVFRNFIGQ GYYGTHTPKV ILRNILENPA WYTAYTPYQA
     EISQGRMEAL INFQTLCADL TGMQIANASL LDEATAAAEA MTLAKRSAKS RSNTFFVHDA
     VHPQTLELLR TRAEPLDIVL RVGTPEEALQ AECFGVLLQY PDSFGHIGDH AALADAVHAQ
     GGLVAVATDL LALTLIAAPG EWGADIVVGN SQRFGVPFGF GGPHAAFMAC RDAYKRSMPG
     RLIGVSIDAA GNPAYRLTLQ TREQHIRREK ATSNICTAQV LLAVMASMYA VYHGPDGLTR
     IARRTHRLAA ILAAALRSAG VTVGERFFDT LHVKAIDANA IHARARAAGI NLRAIDSEAV
     GISLDETSTR ADVVALAALF GAQADVDALD AATADALPQG LLRTTPFLTH PVFNTHHSEH
     ELLRYMRSLA DKDLAMDRTM IPLGSCTMKL NATAEMIPVT WPEFGAIHPL APAEQSAGYA
     QLIDELEAML VECTGYDAVS LQPNSGAQGE YAGLLAIRAY HRSRGEAHRD ICLIPESAHG
     TNPASAQMCG MTVVVTKCDA NGNVDVDDIR AKAEKYSDRL AALMITYPST HGVFEEDVVA
     ICEAVHAHGG QVYTDGANMN ALVGVAKPGK WGSDVSHLNL HKTFCIPHGG GGPGVGPCAV
     KSHLAPYLPK TLGGEGDVGM VSAASYGSAS ILPISWMYVT MMGSAGLRKA TQVALLNANY
     IAKRLAPHYK TLYTGRNGLV AHECILDVRP LEKTSGIGAE DIAKRLIDFG FHAPTLSFPV
     AGTLMVEPTE SESQHELDRF IDAMIQIREE IRAIEDGRLD REDNPLKHAP HTATQVSASE
     WTHAYPRELA AFPLPSLKQQ KYWPPVARVD NVYGDKNVMC ACIPVDAYKE DVEA
 
 
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