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O31646

- MANA1_BACSU

UniProt

O31646 - MANA1_BACSU

Protein

Mannose-6-phosphate isomerase ManA

Gene

manA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    D-mannose 6-phosphate = D-fructose 6-phosphate.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi97 – 971ZincBy similarity
    Metal bindingi110 – 1101ZincBy similarity
    Metal bindingi172 – 1721ZincBy similarity
    Active sitei192 – 1921By similarity

    GO - Molecular functioni

    1. mannose-6-phosphate isomerase activity Source: UniProtKB-EC
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Isomerase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciBSUB:BSU12020-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mannose-6-phosphate isomerase ManA (EC:5.3.1.8)
    Alternative name(s):
    Phosphohexomutase
    Phosphomannose isomerase
    Short name:
    PMI
    Gene namesi
    Name:manA
    Synonyms:pmi, yjdE
    Ordered Locus Names:BSU12020
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU12020. [Micado]

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene are unable to grow in minimal medium with mannose as the sole carbon source. They show impaired growth in rich medium, and impairment increases in the presence of greater than 1.4 mM mannose.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 315315Mannose-6-phosphate isomerase ManAPRO_0000371314Add
    BLAST

    Proteomic databases

    PaxDbiO31646.

    Expressioni

    Inductioni

    Up-regulated by mannose. Is under the control of ManR. Is subject to carbon catabolite repression (CCR) by glucose. Forms part of an operon with manP and yjdF.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU12020.

    Structurei

    3D structure databases

    ProteinModelPortaliO31646.
    SMRiO31646. Positions 2-315.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1482.
    HOGENOMiHOG000054245.
    KOiK01809.
    OMAiPKAKEFP.
    OrthoDBiEOG66MQQS.
    PhylomeDBiO31646.

    Family and domain databases

    Gene3Di2.60.120.10. 2 hits.
    InterProiIPR001250. Man6P_Isoase-1.
    IPR014628. Man6P_isomerase_Firm_short.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view]
    PfamiPF01238. PMI_typeI. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036894. PMI_Firm_short. 1 hit.
    SUPFAMiSSF51182. SSF51182. 1 hit.
    TIGRFAMsiTIGR00218. manA. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    O31646-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTEPLFFKP VFKERIWGGT ALADFGYTIP SQRTGECWAF AAHQNGQSVV    50
    QNGMYKGFTL SELWEHHRHL FGQLEGDRFP LLTKILDADQ DLSVQVHPND 100
    EYANIHENGE LGKTECWYII DCQKDAEIIY GHNATTKEEL TTMIERGEWD 150
    ELLRRVKVKP GDFFYVPSGT VHAIGKGILA LETQQNSDTT YRLYDYDRKD 200
    AEGKLRELHL KKSIEVIEVP SIPERHTVHH EQIEDLLTTT LIECAYFSVG 250
    KWNLSGSASL KQQKPFLLIS VIEGEGRMIS GEYVYPFKKG DHMLLPYGLG 300
    EFKLEGYAEC IVSHL 315
    Length:315
    Mass (Da):36,003
    Last modified:January 1, 1998 - v1
    Checksum:i6848958CF5545064
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL009126 Genomic DNA. Translation: CAB13059.1.
    PIRiH69848.
    RefSeqiNP_389084.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB13059; CAB13059; BSU12020.
    GeneIDi939393.
    KEGGibsu:BSU12020.
    PATRICi18974133. VBIBacSub10457_1259.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL009126 Genomic DNA. Translation: CAB13059.1 .
    PIRi H69848.
    RefSeqi NP_389084.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali O31646.
    SMRi O31646. Positions 2-315.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU12020.

    Proteomic databases

    PaxDbi O31646.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13059 ; CAB13059 ; BSU12020 .
    GeneIDi 939393.
    KEGGi bsu:BSU12020.
    PATRICi 18974133. VBIBacSub10457_1259.

    Organism-specific databases

    GenoListi BSU12020. [Micado ]

    Phylogenomic databases

    eggNOGi COG1482.
    HOGENOMi HOG000054245.
    KOi K01809.
    OMAi PKAKEFP.
    OrthoDBi EOG66MQQS.
    PhylomeDBi O31646.

    Enzyme and pathway databases

    BioCyci BSUB:BSU12020-MONOMER.

    Family and domain databases

    Gene3Di 2.60.120.10. 2 hits.
    InterProi IPR001250. Man6P_Isoase-1.
    IPR014628. Man6P_isomerase_Firm_short.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view ]
    Pfami PF01238. PMI_typeI. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036894. PMI_Firm_short. 1 hit.
    SUPFAMi SSF51182. SSF51182. 1 hit.
    TIGRFAMsi TIGR00218. manA. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    2. "Novel phosphotransferase system genes revealed by genome analysis - the complete complement of PTS proteins encoded within the genome of Bacillus subtilis."
      Reizer J., Bachem S., Reizer A., Arnaud M., Saier M.H. Jr., Stuelke J.
      Microbiology 145:3419-3429(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE NAME.
      Strain: 168.
    3. "Mutations in multidrug efflux homologs, sugar isomerases, and antimicrobial biosynthesis genes differentially elevate activity of the sigma(X) and sigma(W) factors in Bacillus subtilis."
      Turner M.S., Helmann J.D.
      J. Bacteriol. 182:5202-5210(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
      Strain: 168.
    4. "Characterization of a mannose utilization system in Bacillus subtilis."
      Sun T., Altenbuchner J.
      J. Bacteriol. 192:2128-2139(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiMANA1_BACSU
    AccessioniPrimary (citable) accession number: O31646
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 5, 2009
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 90 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3