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Q8RBX6 (Q8RBX6_THETN) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length602 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region2 – 43Acetate binding PDB 3TF0 PDB 3TF1
Region89 – 935Sulfate 2 binding PDB 3IQB

Sites

Metal binding1021Iron (heme axial ligand); via tele nitrogen PDB 1U55 PDB 1XBN PDB 1U4H PDB 1U56 PDB 3EEE PDB 3IQB PDB 3NVR PDB 3NVU PDB 3SJ5 PDB 3TF0 PDB 3TF1 PDB 4FDK
Binding site451Sulfate 1; via carbonyl oxygen PDB 3EEE
Binding site821Acetate PDB 3TF1

Sequences

Sequence LengthMass (Da)Tools
Q8RBX6 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 6CD008747FCBC22E

FASTA60268,053
        10         20         30         40         50         60 
MKGTIVGTWI KTLRDLYGND VVDESLKSVG WEPDRVITPL EDIDDDEVRR IFAKVSEKTG 

        70         80         90        100        110        120 
KNVNEIWREV GRQNIKTFSE WFPSYFAGRR LVNFLMMMDE VHLQLTKMIK GATPPRLIAK 

       130        140        150        160        170        180 
PVAKDAIEME YVSKRKMYDY FLGLIEGSSK FFKEEISVEE VERGEKDGFS RLKVRIKFKN 

       190        200        210        220        230        240 
PVFEYKKNVW GKILGFGFIR SNSFKLALWS FIIGFLVVGF VSSWDLLKSF SGAFIIGAFT 

       250        260        270        280        290        300 
YIFSYILNMP AKNLHEFVKI MGSRNLEEEF KLESGDVFEA IAEELNSVKD TIKKDMLFLK 

       310        320        330        340        350        360 
GGTDDMHNFV HRFNEIAENM KKVSEDISSV VNDVASSTVH QAEEIERAVG ILDENIKKIN 

       370        380        390        400        410        420 
EIAGTSKESN EKLENSIENI KRANTDVTDV AKELSQVEVD FSSIYEMGKV LSDSAKDIMA 

       430        440        450        460        470        480 
IVTTVEEISD QTNLLALNAA IEAARAGEAG RGFAVVAEEV RNLAENSKNA VKTITESLVN 

       490        500        510        520        530        540 
FTGQVENLAE KISAQFERLK KSISTLEKVV EKNTMATEEV AGISSVIVES ANRLYEEAEK 

       550        560        570        580        590        600 
LSEVFGHLEN LAAISEENSA SSEEMSANVT EYSNRIREFI EQIKQMETLV TNFKKELDKY 


KV 

« Hide

References

« Hide 'large scale' references
[1]"A complete sequence of the T. tengcongensis genome."
Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y., Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R. expand/collapse author list , Wang J., Yu J., Yang H.
Genome Res. 12:689-700(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 15242 / JCM 11007 / NBRC 100824 / MB4.
[2]"Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases."
Pellicena P., Karow D.S., Boon E.M., Marletta M.A., Kuriyan J.
Proc. Natl. Acad. Sci. U.S.A. 101:12854-12859(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 1-188 IN COMPLEX WITH HEME.
[3]"Femtomolar sensitivity of a NO sensor from Clostridium botulinum."
Nioche P., Berka V., Vipond J., Minton N., Tsai A.L., Raman C.S.
Science 306:1550-1553(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-191 IN COMPLEX WITH HEME.
[4]"Probing the function of heme distortion in the H-NOX family."
Olea C., Boon E.M., Pellicena P., Kuriyan J., Marletta M.A.
ACS Chem. Biol. 3:703-710(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 1-188 IN COMPLEX WITH HEME AND SULFATE.
[5]"Determinants of ligand affinity and heme reactivity in H-NOX domains."
Weinert E.E., Plate L., Whited C.A., Olea C., Marletta M.A.
Angew. Chem. Int. Ed. 49:720-723(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-188 IN COMPLEX WITH HEME AND SULFATE.
[6]"Ru-porphyrin protein scaffolds for sensing O2."
Winter M.B., McLaurin E.J., Reece S.Y., Olea C., Nocera D.G., Marletta M.A.
J. Am. Chem. Soc. 132:5582-5583(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-188.
[7]"Modulating heme redox potential through protein-induced porphyrin distortion."
Olea C., Kuriyan J., Marletta M.A.
J. Am. Chem. Soc. 132:12794-12795(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 1-188 IN COMPLEX WITH HEME.
[8]"Structural insights into the molecular mechanism of H-NOX activation."
Olea C., Herzik M.A., Kuriyan J., Marletta M.A.
Protein Sci. 19:881-887(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-188.
[9]"Controlling conformational flexibility of an O2-binding H-NOX domain."
Weinert E.E., Phillips-Piro C.M., Tran R., Mathies R.A., Marletta M.A.
Biochemistry 50:6832-6840(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 1-188 IN COMPLEX WITH HEME.
[10]"Tunnels modulate ligand flux in a heme nitric oxide/oxygen binding (H-NOX) domain."
Winter M.B., Herzik M.A., Kuriyan J., Marletta M.A.
Proc. Natl. Acad. Sci. U.S.A. 108:E881-E889(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 1-188 IN COMPLEX WITH ACETATE AND HEME.
[11]"Porphyrin-substituted H-NOX proteins as high-relaxivity MRI contrast agents."
Winter M.B., Klemm P.J., Phillips-Piro C.M., Raymond K.N., Marletta M.A.
Inorg. Chem. 52:2277-2279(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-188.
[12]"Porphyrin ?-stacking in a heme protein scaffold tunes gas ligand affinity."
Weinert E.E., Phillips-Piro C.M., Marletta M.A.
J. Inorg. Biochem. 127:7-12(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-188 IN COMPLEX WITH HEME.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008691 Genomic DNA. Translation: AAM23944.1.
RefSeqNP_622340.1. NC_003869.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1U4HX-ray2.07A/B1-188[»]
1U55X-ray1.77A/B1-188[»]
1U56X-ray1.90A/B1-188[»]
1XBNX-ray2.50A1-191[»]
3EEEX-ray2.12A/B/C/D1-188[»]
3IQBX-ray2.10A1-188[»]
3LAHX-ray2.00A/B1-188[»]
3LAIX-ray2.14A/B/C1-188[»]
3M0BX-ray2.00A1-188[»]
3NVRX-ray2.15A/B1-188[»]
3NVUX-ray2.04A/B1-188[»]
3SJ5X-ray1.67A/B1-188[»]
3TF0X-ray1.74A/B1-188[»]
3TF1X-ray2.04A/B1-188[»]
4FDKX-ray2.10A/B1-188[»]
4IT2X-ray2.10A/B1-188[»]
ProteinModelPortalQ8RBX6.
SMRQ8RBX6. Positions 1-188.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273068.TTE0680.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM23944; AAM23944; TTE0680.
GeneID996654.
KEGGtte:TTE0680.
PATRIC23896032. VBITheTen82880_0678.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000055038.
KOK03406.
OMAFSKWFPS.
OrthoDBEOG6FRCT2.

Family and domain databases

InterProIPR011644. Heme_NO-bd.
IPR004089. MCPsignal_dom.
IPR024096. NO_sig/Golgi_transp_ligand-bd.
[Graphical view]
PfamPF07700. HNOB. 1 hit.
PF00015. MCPsignal. 1 hit.
[Graphical view]
SMARTSM00283. MA. 1 hit.
[Graphical view]
SUPFAMSSF111126. SSF111126. 1 hit.
PROSITEPS50111. CHEMOTAXIS_TRANSDUC_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8RBX6.

Entry information

Entry nameQ8RBX6_THETN
AccessionPrimary (citable) accession number: Q8RBX6
Entry history
Integrated into UniProtKB/TrEMBL: June 1, 2002
Last sequence update: June 1, 2002
Last modified: June 11, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)