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MTNB_BACSU
ID   MTNB_BACSU              Reviewed;         209 AA.
AC   O31668;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Methylthioribulose-1-phosphate dehydratase;
DE            Short=MTRu-1-P dehydratase;
DE            EC=4.2.1.109;
GN   Name=mtnB; Synonyms=ykrY; OrderedLocusNames=BSU13610;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [2]
RP   REVIEW.
RX   PubMed=12022921; DOI=10.1186/1471-2180-2-8;
RA   Sekowska A., Danchin A.;
RT   "The methionine salvage pathway in Bacillus subtilis.";
RL   BMC Microbiol. 2:8-8(2002).
RN   [3]
RP   FUNCTION.
RX   PubMed=14551435; DOI=10.1126/science.1086997;
RA   Ashida H., Saito Y., Kojima C., Kobayashi K., Ogasawara N., Yokota A.;
RT   "A functional link between RuBisCO-like protein of Bacillus and
RT   photosynthetic RuBisCO.";
RL   Science 302:286-290(2003).
RN   [4]
RP   NOMENCLATURE.
RX   PubMed=15102328; DOI=10.1186/1471-2180-4-9;
RA   Sekowska A., Denervaud V., Ashida H., Michoud K., Haas D., Yokota A.,
RA   Danchin A.;
RT   "Bacterial variations on the methionine salvage pathway.";
RL   BMC Microbiol. 4:9-9(2004).
RN   [5]
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=168;
RX   PubMed=18391471; DOI=10.1271/bbb.70651;
RA   Ashida H., Saito Y., Kojima C., Yokota A.;
RT   "Enzymatic characterization of 5-methylthioribulose-1-phosphate dehydratase
RT   of the methionine salvage pathway in Bacillus subtilis.";
RL   Biosci. Biotechnol. Biochem. 72:959-967(2008).
CC   -!- FUNCTION: Catalyzes the dehydration of methylthioribulose-1-phosphate
CC       (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
CC       {ECO:0000269|PubMed:14551435}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-
CC         dioxopentyl phosphate + H2O; Xref=Rhea:RHEA:15549, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:58548, ChEBI:CHEBI:58828; EC=4.2.1.109;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=8.9 uM for S-methyl-5-thio-D-ribulose 1-phosphate (at 25 degrees
CC         Celsius) {ECO:0000269|PubMed:18391471};
CC         Vmax=42.7 umol/min/mg enzyme (at 25 degrees Celsius)
CC         {ECO:0000269|PubMed:18391471};
CC       pH dependence:
CC         Optimum pH is 7.5-8.5. {ECO:0000269|PubMed:18391471};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius. It loses most of its
CC         activity at 55 degrees Celsius. {ECO:0000269|PubMed:18391471};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC       pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC       step 2/6.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:18391471}.
CC   -!- SIMILARITY: Belongs to the aldolase class II family. MtnB subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AL009126; CAB13234.1; -; Genomic_DNA.
DR   PIR; A69864; A69864.
DR   RefSeq; NP_389244.1; NC_000964.3.
DR   RefSeq; WP_003244782.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O31668; -.
DR   SMR; O31668; -.
DR   STRING; 224308.BSU13610; -.
DR   PaxDb; O31668; -.
DR   PRIDE; O31668; -.
DR   EnsemblBacteria; CAB13234; CAB13234; BSU_13610.
DR   GeneID; 939320; -.
DR   KEGG; bsu:BSU13610; -.
DR   PATRIC; fig|224308.179.peg.1478; -.
DR   eggNOG; COG0235; Bacteria.
DR   InParanoid; O31668; -.
DR   OMA; IRGHGLY; -.
DR   PhylomeDB; O31668; -.
DR   BioCyc; BSUB:BSU13610-MON; -.
DR   BioCyc; MetaCyc:BSU13610-MON; -.
DR   UniPathway; UPA00904; UER00875.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0046570; F:methylthioribulose 1-phosphate dehydratase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central.
DR   GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.225.10; -; 1.
DR   HAMAP; MF_01677; Salvage_MtnB; 1.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
DR   InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR   InterPro; IPR017714; MethylthioRu-1-P_deHdtase_MtnB.
DR   PANTHER; PTHR10640; PTHR10640; 1.
DR   Pfam; PF00596; Aldolase_II; 1.
DR   SMART; SM01007; Aldolase_II; 1.
DR   SUPFAM; SSF53639; SSF53639; 1.
DR   TIGRFAMs; TIGR03328; salvage_mtnB; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Lyase; Metal-binding; Methionine biosynthesis;
KW   Reference proteome; Zinc.
FT   CHAIN           1..209
FT                   /note="Methylthioribulose-1-phosphate dehydratase"
FT                   /id="PRO_0000162937"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   209 AA;  23489 MW;  D4E8BE3544026FAB CRC64;
     MAAKQERWRE LAEVKRELAE RDWFPATSGN LSIKVTDEPL TFLVTASGKD KRKETVEDFL
     LVDQNGEPAE SGHSLKPSAE TLLHTHLYNK TNAGCCLHVH TVNNNVISEL YGDQKKITFK
     GQEIIKALGL WEENAEVTVP IIENPAHIPT LAALFAEEIS EDSGAVLIRN HGITAWGKTA
     FEAKRVLEAY EFLFSYHLKL KTLEHQLVK
 
 
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