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Protein

Queuine tRNA-ribosyltransferase

Gene

tgt

Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GUN anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).UniRule annotation1 Publication

Catalytic activityi

Guanine(34) in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7-carbaguanine(34) in tRNA + guanine.UniRule annotation1 Publication

Cofactori

Zn2+UniRule annotation10 PublicationsNote: Binds 1 zinc ion per subunit.UniRule annotation10 Publications

Kineticsi

kcat is 0.0022 sec(-1) with tRNA(Tyr) and guanine as substrates.1 Publication

Manual assertion based on experiment ini

  • Ref.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, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES.

  1. KM=0.2 µM for tRNA(Tyr)1 Publication
  2. KM=0.7 µM for guanine1 Publication

    Pathwayi: tRNA-queuosine biosynthesis

    This protein is involved in the pathway tRNA-queuosine biosynthesis, which is part of tRNA modification.UniRule annotation1 Publication
    View all proteins of this organism that are known to be involved in the pathway tRNA-queuosine biosynthesis and in tRNA modification.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei102Proton acceptorUniRule annotation1 Publication1
    Binding sitei156SubstrateUniRule annotation1 Publication1
    Binding sitei203SubstrateUniRule annotation1 Publication1
    Binding sitei230Substrate; via amide nitrogenUniRule annotation1 Publication1
    Active sitei280NucleophileUniRule annotation1 Publication1
    Metal bindingi318ZincUniRule annotation10 Publications1
    Metal bindingi320ZincUniRule annotation10 Publications1
    Metal bindingi323ZincUniRule annotation10 Publications1
    Metal bindingi349Zinc; via pros nitrogenUniRule annotation10 Publications1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Queuosine biosynthesis, tRNA processing

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi2.4.2.29. 6765.
    UniPathwayiUPA00392.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Queuine tRNA-ribosyltransferaseUniRule annotation (EC:2.4.2.29UniRule annotation)
    Alternative name(s):
    Guanine insertion enzymeUniRule annotation
    tRNA-guanine transglycosylaseUniRule annotation
    Gene namesi
    Name:tgtUniRule annotation
    Ordered Locus Names:ZMO0363
    OrganismiZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
    Taxonomic identifieri264203 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas
    Proteomesi
    • UP000001173 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi103S → A: Strongly reduces activity. 1 Publication1
    Mutagenesisi156D → A: Abolishes catalytic activity. 1 Publication1
    Mutagenesisi280D → N: Abolishes catalytic activity. 1 Publication1

    Chemistry databases

    ChEMBLiCHEMBL2987.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00001355632 – 386Queuine tRNA-ribosyltransferaseAdd BLAST385

    Interactioni

    Subunit structurei

    Homodimer. Within each dimer, one monomer is responsible for RNA recognition and catalysis, while the other monomer binds to the replacement base PreQ1.UniRule annotation2 Publications

    Chemistry databases

    BindingDBiP28720.

    Structurei

    Secondary structure

    1386
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi15 – 22Combined sources8
    Beta strandi25 – 32Combined sources8
    Beta strandi35 – 43Combined sources9
    Beta strandi45 – 50Combined sources6
    Helixi56 – 61Combined sources6
    Beta strandi67 – 70Combined sources4
    Helixi71 – 76Combined sources6
    Turni77 – 79Combined sources3
    Helixi80 – 85Combined sources6
    Helixi89 – 93Combined sources5
    Beta strandi99 – 102Combined sources4
    Helixi107 – 111Combined sources5
    Helixi112 – 114Combined sources3
    Beta strandi115 – 117Combined sources3
    Beta strandi122 – 125Combined sources4
    Turni127 – 129Combined sources3
    Beta strandi132 – 135Combined sources4
    Helixi137 – 147Combined sources11
    Beta strandi150 – 153Combined sources4
    Helixi165 – 188Combined sources24
    Helixi190 – 195Combined sources6
    Beta strandi197 – 202Combined sources6
    Helixi208 – 221Combined sources14
    Beta strandi224 – 228Combined sources5
    Beta strandi232 – 234Combined sources3
    Helixi237 – 247Combined sources11
    Helixi248 – 250Combined sources3
    Beta strandi253 – 255Combined sources3
    Beta strandi257 – 259Combined sources3
    Helixi265 – 273Combined sources9
    Beta strandi278 – 280Combined sources3
    Helixi283 – 289Combined sources7
    Beta strandi291 – 293Combined sources3
    Beta strandi298 – 301Combined sources4
    Helixi305 – 307Combined sources3
    Beta strandi314 – 317Combined sources4
    Helixi321 – 325Combined sources5
    Helixi328 – 337Combined sources10
    Helixi340 – 366Combined sources27
    Helixi370 – 381Combined sources12

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    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[»]
    4KWOX-ray1.32A1-386[»]
    4L56X-ray1.70A1-386[»]
    4LBUX-ray1.17A1-386[»]
    4LEQX-ray1.40A1-386[»]
    4PUJX-ray1.42A1-386[»]
    4PUKX-ray1.49A1-386[»]
    4PULX-ray1.65A1-386[»]
    4PUMX-ray1.93A1-386[»]
    4PUNX-ray1.25A1-386[»]
    4Q4MX-ray1.62A1-386[»]
    4Q4OX-ray1.35A1-386[»]
    4Q4PX-ray1.54A1-386[»]
    4Q4QX-ray1.41A1-386[»]
    4Q4RX-ray1.45A1-386[»]
    4Q4SX-ray1.25A1-386[»]
    4Q8MX-ray1.24A1-386[»]
    4Q8NX-ray1.45A1-386[»]
    4Q8OX-ray1.89A1-386[»]
    4Q8PX-ray1.45A1-386[»]
    4Q8QX-ray1.72A1-386[»]
    4Q8TX-ray1.40A1-386[»]
    4Q8UX-ray1.31A1-386[»]
    4Q8VX-ray1.40A1-386[»]
    4Q8WX-ray1.14A1-386[»]
    5JXQX-ray1.20A1-386[»]
    ProteinModelPortaliP28720.
    SMRiP28720.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP28720.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni102 – 106Substrate bindingUniRule annotation1 Publication5
    Regioni261 – 267RNA bindingUniRule annotation1 Publication7
    Regioni285 – 289RNA binding; important for wobble base 34 recognitionUniRule annotation1 Publication5

    Sequence similaritiesi

    Belongs to the queuine tRNA-ribosyltransferase family.UniRule annotation

    Phylogenomic databases

    HOGENOMiHOG000223473.
    KOiK00773.
    OMAiGIDLFDC.

    Family and domain databases

    Gene3Di3.20.20.105. 1 hit.
    HAMAPiMF_00168. Q_tRNA_Tgt. 1 hit.
    InterProiIPR004803. Queuine_tRNA-ribosylTrfase.
    IPR002616. tRNA_ribo_trans-like.
    [Graphical view]
    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

            10         20         30         40         50
    MVEATAQETD RPRFSFSIAA REGKARTGTI EMKRGVIRTP AFMPVGTAAT
    60 70 80 90 100
    VKALKPETVR ATGADIILGN TYHLMLRPGA ERIAKLGGLH SFMGWDRPIL
    110 120 130 140 150
    TDSGGYQVMS LSSLTKQSEE GVTFKSHLDG SRHMLSPERS IEIQHLLGSD
    160 170 180 190 200
    IVMAFDECTP YPATPSRAAS SMERSMRWAK RSRDAFDSRK EQAENAALFG
    210 220 230 240 250
    IQQGSVFENL RQQSADALAE IGFDGYAVGG LAVGEGQDEM FRVLDFSVPM
    260 270 280 290 300
    LPDDKPHYLM GVGKPDDIVG AVERGIDMFD CVLPTRSGRN GQAFTWDGPI
    310 320 330 340 350
    NIRNARFSED LTPLDSECHC AVCQKWSRAY IHHLIRAGEI LGAMLMTEHN
    360 370 380
    IAFYQQLMQK IRDSISEGRF SQFAQDFRAR YFARNS
    Length:386
    Mass (Da):42,843
    Last modified:January 23, 2007 - v4
    Checksum:i26754E08600BD941
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti312T → K (PubMed:7665516).Curated1
    Sequence conflicti312T → K (Ref. 2) Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    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[»]
    4KWOX-ray1.32A1-386[»]
    4L56X-ray1.70A1-386[»]
    4LBUX-ray1.17A1-386[»]
    4LEQX-ray1.40A1-386[»]
    4PUJX-ray1.42A1-386[»]
    4PUKX-ray1.49A1-386[»]
    4PULX-ray1.65A1-386[»]
    4PUMX-ray1.93A1-386[»]
    4PUNX-ray1.25A1-386[»]
    4Q4MX-ray1.62A1-386[»]
    4Q4OX-ray1.35A1-386[»]
    4Q4PX-ray1.54A1-386[»]
    4Q4QX-ray1.41A1-386[»]
    4Q4RX-ray1.45A1-386[»]
    4Q4SX-ray1.25A1-386[»]
    4Q8MX-ray1.24A1-386[»]
    4Q8NX-ray1.45A1-386[»]
    4Q8OX-ray1.89A1-386[»]
    4Q8PX-ray1.45A1-386[»]
    4Q8QX-ray1.72A1-386[»]
    4Q8TX-ray1.40A1-386[»]
    4Q8UX-ray1.31A1-386[»]
    4Q8VX-ray1.40A1-386[»]
    4Q8WX-ray1.14A1-386[»]
    5JXQX-ray1.20A1-386[»]
    ProteinModelPortaliP28720.
    SMRiP28720.
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry databases

    BindingDBiP28720.
    ChEMBLiCHEMBL2987.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Phylogenomic databases

    HOGENOMiHOG000223473.
    KOiK00773.
    OMAiGIDLFDC.

    Enzyme and pathway databases

    UniPathwayiUPA00392.
    BRENDAi2.4.2.29. 6765.

    Miscellaneous databases

    EvolutionaryTraceiP28720.
    PROiP28720.

    Family and domain databases

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

    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: November 2, 2016
    This is version 145 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.