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Q5QZ47 (Q5QZ47_IDILO) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
DNA gyrase subunit A HAMAP MF_01897

EC=5.99.1.3 HAMAP MF_01897
Gene names
Name:gyrA HAMAP MF_01897 EMBL AAV82200.1
Ordered Locus Names:IL1360
OrganismIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP]
Taxonomic identifier283942 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina

Protein attributes

Sequence length828 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings By similarity. SAAS SAAS006691 HAMAP MF_01897

Catalytic activity

ATP-dependent breakage, passage and rejoining of double-stranded DNA. SAAS SAAS006691 HAMAP MF_01897

Subunit structure

Made up of two chains. The A chain is responsible for DNA breakage and rejoining; the B chain catalyzes ATP hydrolysis. The enzyme forms an A2B2 tetramer By similarity. HAMAP MF_01897

Subcellular location

Cytoplasm By similarity SAAS SAAS006691 HAMAP MF_01897.

Sequence similarities

Belongs to the topoisomerase GyrA/ParC subunit family. HAMAP MF_01897

Sequences

Sequence LengthMass (Da)Tools
Q5QZ47 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 30FBA9962C354B71

FASTA82892,338
        10         20         30         40         50         60 
MSELRNDFNK PYKKSARVVG DVIGKYHPHG DSAVYDTIVR MAQNFSLRYM LVDGQGNFGS 

        70         80         90        100        110        120 
VDGDSAAAMR YTEIRMAKIA HQLLADLDKE TVDFVDNYDG TERIPDVLPT RVPNLLVNGS 

       130        140        150        160        170        180 
SGIAVGMATN IPPHNLTEVV DGALAMIDNP DIDVEGLMEY IPGPDFPTAA TISGRSGIVE 

       190        200        210        220        230        240 
AYKTGRGRIH LRAQAEIEVD EKTGKETIIV TEIPYQVNKA RLIEKIAELV KEKRVEGISA 

       250        260        270        280        290        300 
LRDESDKDGM RIVIEIRRGD VGEVVLNHLY ANTQLQVVFG INMVALDKGQ PRLFNLRDML 

       310        320        330        340        350        360 
DCFVRHRREV VTRRSVYELR KARERAHILE GLAISLANID EIIELIRRSP TPAEAKAGLI 

       370        380        390        400        410        420 
ARAWQLGDVA AMLETAGVDA ARPDHLPEEY GIRDGNYHLT EEQAQAILDL RLHKLTGLEH 

       430        440        450        460        470        480 
EKILDEYKGL LEQIAELLHI LNSSERLMEV IREELVEIRN NFGDERKTDI TAAAHDISME 

       490        500        510        520        530        540 
DLINEEDVVL TLSHEGYVKY QPLTEYEAQR RGGKGKAATK MKDEDFIERL WVANTHDTIL 

       550        560        570        580        590        600 
CFSTRGRIYW MKVYQLPLAS RASRGKPIVN LLPLEADERI TAILPTRDYP EDKFVVMATR 

       610        620        630        640        650        660 
KGTIKKTPLP EYSRPRNGGI IALNLVDDDE LIGVDITDGN GEIMLFSDAG KVVRFAEEQV 

       670        680        690        700        710        720 
RSMGRTATGV RGIRLEEGQR VVSLIVPREY EEEEANVLTV TENGYGKRTP LSEYPAKSRA 

       730        740        750        760        770        780 
TKGVVSIKVS ERNGSVVGAM EVIDGNEIML ISNKGTLVRT RVNEVSTVGR NTQGVRLIRT 

       790        800        810        820 
ADDEKVVGLQ RIDEIDEDEV LIDGEVVAEE GETAAEDNTE NQEGSDES 

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References

[1]"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy."
Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. expand/collapse author list , Aizawa S., Shibata S., Malahoff A., Alam M.
Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed: 15596722] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017340 Genomic DNA. Translation: AAV82200.1.
RefSeqYP_155749.1. NC_006512.1.

3D structure databases

ProteinModelPortalQ5QZ47.
SMRQ5QZ47. Positions 1-471, 485-794.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3173553.
GenomeReviewsGene locus IL1360 in contig AE017340_GR.
KEGGilo:IL1360.
NMPDRfig|283942.3.peg.1612.
PATRIC22140795. VBIIdiLoi21852_1361.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG635183.
OMATSIPPHR.

Family and domain databases

HAMAPMF_01897. GyrA.
[Tree]
InterProIPR005743. GyrA.
IPR006691. GyrA/parC_pinwhl.
IPR002205. Topo_IIA_A/C.
IPR013758. Topo_IIA_A/C_ab.
IPR013757. Topo_IIA_A_a.
IPR013760. Topo_IIA_cen.
[Graphical view]
Gene3DG3DSA:3.90.199.10. Topo_IIA_A/C_ab. 1 hit.
G3DSA:1.10.268.10. Topo_IIA_A_a. 1 hit.
KOK02469.
PfamPF03989. DNA_gyraseA_C. 6 hits.
PF00521. DNA_topoisoIV. 1 hit.
[Graphical view]
SMARTSM00434. TOP4c. 1 hit.
[Graphical view]
SUPFAMSSF56719. Topo_IIA_cen. 1 hit.
TIGRFAMsTIGR01063. GyrA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ5QZ47_IDILO
AccessionPrimary (citable) accession number: Q5QZ47
Entry history
Integrated into UniProtKB/TrEMBL: January 4, 2005
Last sequence update: January 4, 2005
Last modified: January 25, 2012
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)