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P28720

- TGT_ZYMMO

UniProt

P28720 - TGT_ZYMMO

Protein

Queuine tRNA-ribosyltransferase

Gene

tgt

Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    • Comment

    Functioni

    Exchanges the guanine residue with 7-aminomethyl-7-deazaguanine in tRNAs with GUN anticodons (tRNA-Asp, -Asn, -His and -Tyr). After this exchange, a cyclopentendiol moiety is attached to the 7-aminomethyl group of 7-deazaguanine, resulting in the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).

    Catalytic activityi

    Guanine(34) in tRNA + queuine = queuosine(34) in tRNA + guanine.
    Guanine(34) in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7-carbaguanine(34) in tRNA + guanine.

    Cofactori

    Binds 1 zinc ion per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei102 – 1021Nucleophile
    Binding sitei103 – 1031Substrate
    Metal bindingi318 – 3181Zinc
    Metal bindingi320 – 3201Zinc
    Metal bindingi323 – 3231Zinc
    Metal bindingi349 – 3491Zinc

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. queuine tRNA-ribosyltransferase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. queuosine biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Queuosine biosynthesis, tRNA processing

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00392.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Queuine tRNA-ribosyltransferase (EC:2.4.2.29)
    Alternative name(s):
    Guanine insertion enzyme
    tRNA-guanine transglycosylase
    Gene namesi
    Name:tgt
    Ordered Locus Names:ZMO0363
    OrganismiZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
    Taxonomic identifieri264203 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas
    ProteomesiUP000001173: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi103 – 1031S → A: Strongly reduces activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 386385Queuine tRNA-ribosyltransferasePRO_0000135563Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    STRINGi264203.ZMO0363.

    Structurei

    Secondary structure

    1
    386
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi15 – 228
    Beta strandi25 – 328
    Beta strandi35 – 439
    Beta strandi45 – 506
    Helixi56 – 616
    Beta strandi67 – 704
    Helixi71 – 766
    Turni77 – 793
    Helixi80 – 856
    Helixi89 – 935
    Beta strandi99 – 1024
    Helixi105 – 1084
    Turni109 – 1113
    Helixi112 – 1143
    Beta strandi116 – 1183
    Beta strandi122 – 1254
    Turni127 – 1293
    Beta strandi132 – 1354
    Helixi137 – 14711
    Beta strandi150 – 1534
    Helixi165 – 18723
    Helixi190 – 1956
    Beta strandi197 – 2026
    Helixi208 – 22114
    Beta strandi224 – 2285
    Beta strandi232 – 2354
    Helixi237 – 24711
    Helixi248 – 2503
    Beta strandi253 – 2553
    Beta strandi257 – 2593
    Helixi265 – 2739
    Beta strandi278 – 2803
    Helixi283 – 2897
    Beta strandi290 – 2934
    Beta strandi298 – 3014
    Helixi305 – 3073
    Beta strandi314 – 3174
    Helixi321 – 3255
    Helixi328 – 3369
    Helixi340 – 36627
    Helixi370 – 38112

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EFZX-ray2.00A1-386[»]
    1ENUX-ray1.95A1-386[»]
    1F3EX-ray1.85A1-386[»]
    1K4GX-ray1.70A1-386[»]
    1K4HX-ray1.80A1-386[»]
    1N2VX-ray2.10A1-386[»]
    1OZMX-ray1.95A2-386[»]
    1OZQX-ray1.90A2-386[»]
    1P0BX-ray1.70A2-386[»]
    1P0DX-ray1.90A2-386[»]
    1P0EX-ray2.40A2-386[»]
    1PUDX-ray1.85A1-386[»]
    1PXGX-ray1.70A2-383[»]
    1Q2RX-ray2.90A/B/C/D1-386[»]
    1Q2SX-ray3.20A/B/C/D1-386[»]
    1Q4WX-ray1.93A1-386[»]
    1Q63X-ray1.85A1-386[»]
    1Q65X-ray2.10A1-386[»]
    1Q66X-ray1.75A1-386[»]
    1R5YX-ray1.20A1-386[»]
    1S38X-ray1.81A1-386[»]
    1S39X-ray1.95A1-386[»]
    1WKDX-ray2.60A1-386[»]
    1WKEX-ray2.20A1-386[»]
    1WKFX-ray2.20A1-386[»]
    1Y5VX-ray1.58A2-386[»]
    1Y5WX-ray1.58A2-386[»]
    1Y5XX-ray2.10A/D2-386[»]
    2BBFX-ray1.70A1-386[»]
    2NQZX-ray1.46A2-386[»]
    2NSOX-ray1.60A1-386[»]
    2OKOX-ray1.50A2-386[»]
    2POTX-ray1.80A1-386[»]
    2PWUX-ray1.77A1-386[»]
    2PWVX-ray1.70A1-386[»]
    2QIIX-ray1.70A1-386[»]
    2QZRX-ray1.95A2-386[»]
    2Z1VX-ray1.55A1-386[»]
    2Z1WX-ray1.63A1-386[»]
    2Z1XX-ray1.63A1-386[»]
    2Z7KX-ray1.28A1-386[»]
    3BL3X-ray2.25A1-386[»]
    3BLDX-ray1.19A1-386[»]
    3BLLX-ray1.26A1-386[»]
    3BLOX-ray1.60A1-386[»]
    3C2NX-ray1.58A1-386[»]
    3C2YX-ray1.78A1-386[»]
    3EOSX-ray1.78A1-386[»]
    3EOUX-ray1.93A1-386[»]
    3GC4X-ray1.80A1-386[»]
    3GC5X-ray1.40A1-386[»]
    3GE7X-ray1.50A1-386[»]
    3HFYX-ray2.00A1-386[»]
    3RR4X-ray1.68A1-386[»]
    3S1GX-ray1.82A1-386[»]
    3SM0X-ray1.57A1-386[»]
    3TLLX-ray1.37A1-386[»]
    3UNTX-ray1.80A1-386[»]
    3UVIX-ray1.55A1-386[»]
    4DXXX-ray1.66A1-386[»]
    4DY1X-ray2.04A1-386[»]
    4E2VX-ray1.18A1-386[»]
    4FPSX-ray1.45A1-386[»]
    4FR1X-ray1.74A1-386[»]
    4FR6X-ray1.59A1-386[»]
    4FSAX-ray1.62A1-386[»]
    4GCXX-ray1.42A1-386[»]
    4GD0X-ray1.29A1-386[»]
    4GG9X-ray1.48A1-386[»]
    4GH1X-ray1.45A1-386[»]
    4GH3X-ray2.06A1-386[»]
    4GHRX-ray2.00A1-386[»]
    4GI4X-ray1.97A1-386[»]
    4GIYX-ray1.75A1-386[»]
    4GKTX-ray1.53A1-386[»]
    4H6EX-ray1.42A1-386[»]
    4H7ZX-ray1.68A1-386[»]
    4HQVX-ray1.66A2-386[»]
    4HSHX-ray1.56A2-386[»]
    4HTBX-ray1.90A1-386[»]
    4HVXX-ray1.82A1-386[»]
    4IPPX-ray1.33A1-386[»]
    4JBRX-ray2.92A1-386[»]
    4Q4QX-ray1.41A1-386[»]
    4Q4RX-ray1.45A1-386[»]
    4Q4SX-ray1.25A1-386[»]
    ProteinModelPortaliP28720.
    SMRiP28720. Positions 11-386.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP28720.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0343.
    HOGENOMiHOG000223473.
    KOiK00773.

    Family and domain databases

    Gene3Di3.20.20.105. 1 hit.
    HAMAPiMF_00168. Q_tRNA_Tgt.
    InterProiIPR004803. Queuine_tRNA-ribosylTrfase.
    IPR002616. tRNA_ribo_trans-like.
    [Graphical view]
    PANTHERiPTHR11962. PTHR11962. 1 hit.
    PfamiPF01702. TGT. 1 hit.
    [Graphical view]
    SUPFAMiSSF51713. SSF51713. 1 hit.
    TIGRFAMsiTIGR00430. Q_tRNA_tgt. 1 hit.
    TIGR00449. tgt_general. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P28720-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVEATAQETD RPRFSFSIAA REGKARTGTI EMKRGVIRTP AFMPVGTAAT    50
    VKALKPETVR ATGADIILGN TYHLMLRPGA ERIAKLGGLH SFMGWDRPIL 100
    TDSGGYQVMS LSSLTKQSEE GVTFKSHLDG SRHMLSPERS IEIQHLLGSD 150
    IVMAFDECTP YPATPSRAAS SMERSMRWAK RSRDAFDSRK EQAENAALFG 200
    IQQGSVFENL RQQSADALAE IGFDGYAVGG LAVGEGQDEM FRVLDFSVPM 250
    LPDDKPHYLM GVGKPDDIVG AVERGIDMFD CVLPTRSGRN GQAFTWDGPI 300
    NIRNARFSED LTPLDSECHC AVCQKWSRAY IHHLIRAGEI LGAMLMTEHN 350
    IAFYQQLMQK IRDSISEGRF SQFAQDFRAR YFARNS 386
    Length:386
    Mass (Da):42,843
    Last modified:January 23, 2007 - v4
    Checksum:i26754E08600BD941
    GO

    Sequence cautioni

    The sequence Z11910 differs from that shown. Reason: Frameshift at several positions.
    The sequence AAA27704.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAA27705.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAG29862.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti312 – 3121T → K(PubMed:7665516)Curated
    Sequence conflicti312 – 3121T → K1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33777 Genomic DNA. Translation: AAA27704.1. Different initiation.
    L33777 Genomic DNA. Translation: AAA27705.1. Different initiation.
    AF313764 Genomic DNA. Translation: AAG29862.1. Different initiation.
    AE008692 Genomic DNA. Translation: AAV88987.2.
    Z11910 Genomic DNA. No translation available.
    PIRiT46898.
    RefSeqiYP_162098.2. NC_006526.2.

    Genome annotation databases

    EnsemblBacteriaiAAV88987; AAV88987; ZMO0363.
    GeneIDi3188564.
    KEGGizmo:ZMO0363.
    PATRICi32566062. VBIZymMob102260_0345.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33777 Genomic DNA. Translation: AAA27704.1 . Different initiation.
    L33777 Genomic DNA. Translation: AAA27705.1 . Different initiation.
    AF313764 Genomic DNA. Translation: AAG29862.1 . Different initiation.
    AE008692 Genomic DNA. Translation: AAV88987.2 .
    Z11910 Genomic DNA. No translation available.
    PIRi T46898.
    RefSeqi YP_162098.2. NC_006526.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EFZ X-ray 2.00 A 1-386 [» ]
    1ENU X-ray 1.95 A 1-386 [» ]
    1F3E X-ray 1.85 A 1-386 [» ]
    1K4G X-ray 1.70 A 1-386 [» ]
    1K4H X-ray 1.80 A 1-386 [» ]
    1N2V X-ray 2.10 A 1-386 [» ]
    1OZM X-ray 1.95 A 2-386 [» ]
    1OZQ X-ray 1.90 A 2-386 [» ]
    1P0B X-ray 1.70 A 2-386 [» ]
    1P0D X-ray 1.90 A 2-386 [» ]
    1P0E X-ray 2.40 A 2-386 [» ]
    1PUD X-ray 1.85 A 1-386 [» ]
    1PXG X-ray 1.70 A 2-383 [» ]
    1Q2R X-ray 2.90 A/B/C/D 1-386 [» ]
    1Q2S X-ray 3.20 A/B/C/D 1-386 [» ]
    1Q4W X-ray 1.93 A 1-386 [» ]
    1Q63 X-ray 1.85 A 1-386 [» ]
    1Q65 X-ray 2.10 A 1-386 [» ]
    1Q66 X-ray 1.75 A 1-386 [» ]
    1R5Y X-ray 1.20 A 1-386 [» ]
    1S38 X-ray 1.81 A 1-386 [» ]
    1S39 X-ray 1.95 A 1-386 [» ]
    1WKD X-ray 2.60 A 1-386 [» ]
    1WKE X-ray 2.20 A 1-386 [» ]
    1WKF X-ray 2.20 A 1-386 [» ]
    1Y5V X-ray 1.58 A 2-386 [» ]
    1Y5W X-ray 1.58 A 2-386 [» ]
    1Y5X X-ray 2.10 A/D 2-386 [» ]
    2BBF X-ray 1.70 A 1-386 [» ]
    2NQZ X-ray 1.46 A 2-386 [» ]
    2NSO X-ray 1.60 A 1-386 [» ]
    2OKO X-ray 1.50 A 2-386 [» ]
    2POT X-ray 1.80 A 1-386 [» ]
    2PWU X-ray 1.77 A 1-386 [» ]
    2PWV X-ray 1.70 A 1-386 [» ]
    2QII X-ray 1.70 A 1-386 [» ]
    2QZR X-ray 1.95 A 2-386 [» ]
    2Z1V X-ray 1.55 A 1-386 [» ]
    2Z1W X-ray 1.63 A 1-386 [» ]
    2Z1X X-ray 1.63 A 1-386 [» ]
    2Z7K X-ray 1.28 A 1-386 [» ]
    3BL3 X-ray 2.25 A 1-386 [» ]
    3BLD X-ray 1.19 A 1-386 [» ]
    3BLL X-ray 1.26 A 1-386 [» ]
    3BLO X-ray 1.60 A 1-386 [» ]
    3C2N X-ray 1.58 A 1-386 [» ]
    3C2Y X-ray 1.78 A 1-386 [» ]
    3EOS X-ray 1.78 A 1-386 [» ]
    3EOU X-ray 1.93 A 1-386 [» ]
    3GC4 X-ray 1.80 A 1-386 [» ]
    3GC5 X-ray 1.40 A 1-386 [» ]
    3GE7 X-ray 1.50 A 1-386 [» ]
    3HFY X-ray 2.00 A 1-386 [» ]
    3RR4 X-ray 1.68 A 1-386 [» ]
    3S1G X-ray 1.82 A 1-386 [» ]
    3SM0 X-ray 1.57 A 1-386 [» ]
    3TLL X-ray 1.37 A 1-386 [» ]
    3UNT X-ray 1.80 A 1-386 [» ]
    3UVI X-ray 1.55 A 1-386 [» ]
    4DXX X-ray 1.66 A 1-386 [» ]
    4DY1 X-ray 2.04 A 1-386 [» ]
    4E2V X-ray 1.18 A 1-386 [» ]
    4FPS X-ray 1.45 A 1-386 [» ]
    4FR1 X-ray 1.74 A 1-386 [» ]
    4FR6 X-ray 1.59 A 1-386 [» ]
    4FSA X-ray 1.62 A 1-386 [» ]
    4GCX X-ray 1.42 A 1-386 [» ]
    4GD0 X-ray 1.29 A 1-386 [» ]
    4GG9 X-ray 1.48 A 1-386 [» ]
    4GH1 X-ray 1.45 A 1-386 [» ]
    4GH3 X-ray 2.06 A 1-386 [» ]
    4GHR X-ray 2.00 A 1-386 [» ]
    4GI4 X-ray 1.97 A 1-386 [» ]
    4GIY X-ray 1.75 A 1-386 [» ]
    4GKT X-ray 1.53 A 1-386 [» ]
    4H6E X-ray 1.42 A 1-386 [» ]
    4H7Z X-ray 1.68 A 1-386 [» ]
    4HQV X-ray 1.66 A 2-386 [» ]
    4HSH X-ray 1.56 A 2-386 [» ]
    4HTB X-ray 1.90 A 1-386 [» ]
    4HVX X-ray 1.82 A 1-386 [» ]
    4IPP X-ray 1.33 A 1-386 [» ]
    4JBR X-ray 2.92 A 1-386 [» ]
    4Q4Q X-ray 1.41 A 1-386 [» ]
    4Q4R X-ray 1.45 A 1-386 [» ]
    4Q4S X-ray 1.25 A 1-386 [» ]
    ProteinModelPortali P28720.
    SMRi P28720. Positions 11-386.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 264203.ZMO0363.

    Chemistry

    BindingDBi P28720.
    ChEMBLi CHEMBL2987.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAV88987 ; AAV88987 ; ZMO0363 .
    GeneIDi 3188564.
    KEGGi zmo:ZMO0363.
    PATRICi 32566062. VBIZymMob102260_0345.

    Phylogenomic databases

    eggNOGi COG0343.
    HOGENOMi HOG000223473.
    KOi K00773.

    Enzyme and pathway databases

    UniPathwayi UPA00392 .

    Miscellaneous databases

    EvolutionaryTracei P28720.

    Family and domain databases

    Gene3Di 3.20.20.105. 1 hit.
    HAMAPi MF_00168. Q_tRNA_Tgt.
    InterProi IPR004803. Queuine_tRNA-ribosylTrfase.
    IPR002616. tRNA_ribo_trans-like.
    [Graphical view ]
    PANTHERi PTHR11962. PTHR11962. 1 hit.
    Pfami PF01702. TGT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51713. SSF51713. 1 hit.
    TIGRFAMsi TIGR00430. Q_tRNA_tgt. 1 hit.
    TIGR00449. tgt_general. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis and overexpression of the Zymomonas mobilis tgt gene encoding tRNA-guanine transglycosylase: purification and biochemical characterization of the enzyme."
      Reuter K.K.H., Ficner R.
      J. Bacteriol. 177:5284-5288(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-7, CHARACTERIZATION.
    2. "Sequence analysis of 44B6 fosmid clone of Zymomonas mobilis ZM4."
      Ahn J.Y., Kang H.S.
      Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 31821 / ZM4 / CP4.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 31821 / ZM4 / CP4.
    4. "Cloning and molecular characterization of the DNA ligase gene (lig) from Zymomonas mobilis."
      Shark K.B., Conway T.
      FEMS Microbiol. Lett. 75:19-26(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 31821 / ZM4 / CP4.
    5. "Crystal structure of tRNA-guanine transglycosylase: RNA modification by base exchange."
      Romier C., Reuter K., Suck D., Ficner R.
      EMBO J. 15:2850-2857(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
    6. "Mutagenesis and crystallographic studies of Zymomonas mobilis tRNA-guanine transglycosylase to elucidate the role of serine 103 for enzymatic activity."
      Graedler U., Ficner R., Garcia G.A., Stubbs M.T., Klebe G., Reuter K.
      FEBS Lett. 454:142-146(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 11-382, MUTAGENESIS OF SER-103.
    7. "A new target for shigellosis: rational design and crystallographic studies of inhibitors of tRNA-guanine transglycosylase."
      Graedler U., Gerber H.-D., Goodenough-Lashua D.M., Garcia G.A., Ficner R., Reuter K., Stubbs M.T., Klebe G.
      J. Mol. Biol. 306:455-467(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
    8. "De novo design, synthesis, and in vitro evaluation of inhibitors for prokaryotic tRNA-guanine transglycosylase: a dramatic sulfur effect on binding affinity."
      Meyer E.A., Brenk R., Castellano R.K., Furler M., Klebe G., Diederich F.
      ChemBioChem 3:250-253(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 12-386.
    9. "Virtual screening for submicromolar leads of tRNA-guanine transglycosylase based on a new unexpected binding mode detected by crystal structure analysis."
      Brenk R., Naerum L., Graedler U., Gerber H.-D., Garcia G.A., Reuter K., Stubbs M.T., Klebe G.
      J. Med. Chem. 46:1133-1143(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 12-386.

    Entry informationi

    Entry nameiTGT_ZYMMO
    AccessioniPrimary (citable) accession number: P28720
    Secondary accession number(s): Q5NQL7, Q60247, Q9F5L7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 128 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3