(data stored in SCRATCH3701 zone)

HOGENOM6: ALDEN1_2_PE1814

ID   ALDEN1_2_PE1814                      STANDARD;      PRT;   896 AA.
AC   ALDEN1_2_PE1814; E8TXE6;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   SubName: Full=DNA gyrase, A subunit; EC=5.99.1 3; (ALDEN1_2.PE1814).
GN   OrderedLocusNames=Alide_1855;
OS   ALICYCLIPHILUS DENITRIFICANS BC.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Alicycliphilus.
OX   NCBI_TaxID=596153;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ALDEN1_2.PE1814.
CC       Alicycliphilus denitrificans BC chromosome, complete genome.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:E8TXE6_ALIDB
CC   -!- FUNCTION: DNA gyrase negatively supercoils closed circular double-
CC       stranded DNA in an ATP-dependent manner and also catalyzes the
CC       interconversion of other topological isomers of double-stranded
CC       DNA rings, including catenanes and knotted rings (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
CC       of double-stranded DNA.
CC   -!- SUBUNIT: Made up of two chains. The A chain is responsible for DNA
CC       breakage and rejoining; the B chain catalyzes ATP hydrolysis. The
CC       enzyme forms an A2B2 tetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- GENE_FAMILY: HOG000076278 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; E8TXE6; -.
DR   EMBL; CP002449; ADU99601.1; -; Genomic_DNA.
DR   RefSeq; YP_004126489.1; NC_014910.1.
DR   GeneID; 10103904; -.
DR   GenomeReviews; CP002449_GR; Alide_1855.
DR   KEGG; adn:Alide_1855; -.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase (ATP-hydrolyzing) activity; IEA:EC.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   InterPro; IPR020899; Arg_repress_C.
DR   InterPro; IPR005743; GyrA.
DR   InterPro; IPR006691; GyrA/parC_pinwhl.
DR   InterPro; IPR002205; Topo_IIA_A/C.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a.
DR   InterPro; IPR013760; Topo_IIA_cen.
DR   Gene3D; G3DSA:3.30.1360.40; Arg_repress; 1.
DR   Gene3D; G3DSA:3.90.199.10; Topo_IIA_A/C_ab; 1.
DR   Gene3D; G3DSA:1.10.268.10; Topo_IIA_A_a; 1.
DR   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF56719; Topo_IIA_cen; 1.
DR   TIGRFAMs; TIGR01063; GyrA; 1.
DR   HOGENOMDNA; ALDEN1_2.PE1814; -.
DR   PRODOM; ALDEN1_2_PE1814.
DR   SWISS-2DPAGE; ALDEN1_2_PE1814.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   896 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVLHLKWLFP AVSTAVVMTQ FAKETLPISL EEEMRRSYLD YAMSVIVGRA LPDARDGLKP
     VHRRVLYAMH ELNNDWNRPY KKSARIVGDV IGKYHPHGDS AVYDTIVRMA QDFSLRHMLV
     DGQGNFGSVD GDNAAAMRYT EIRLAKIAHE MLADIDKETV DFGPNYDGSE KEPLVLPSRL
     PNLLVNGSAG IAVGMATNIP PHNLNEVVDA CLHLLRNPES SIDELMEIIP APDFPTAGII
     YGIQGVKDGY RTGRGKVVMR AKVHFEDIDR GQRQAIIVDE LPYQVNKKTL QERMAELVHE
     KKLEGISHIQ DESDKSGMRL VIELKRGEVP EVVLNNLYKQ TQLQDTFGMN MVALVDGQPK
     LCNLKELIEV FLQHRREVVT RRTVFELRKA RERGHVLEGL AVALANIDEF IRIIRESPTP
     PVAKAELMAR SWDSQLVREM LTRTREDGGV VNADDYRPEG LEREFGMQES GLYRLSDTQA
     QEILQMRLQR LTGLEQDKIV AEYKDVMAVI ENLLDILAKP ARVSTIIGEE LSALRQEFGQ
     TRLGARRSTI EHSAQDLSTE DLITPTDMVV TLSHTGYIKS QPLSEYRAQK RGGRGKQATA
     TKEDDWIDQL FIANTHDYIL CFSNRGRLYW LKVWEVPAGS RNSRGRPIVN MFPLQEGEKI
     NVVLPLTGEM RSFPADRYVF MATSMGTVKK TALDEFSNPR KAGIIAVGLD EGDYLIGAAL
     TDGEHDVMLF SDSGKAVRFD ENDVRPMGRN ARGVKGMQLE DGQSVIAMLV AEDENQSVLT
     ATENGYGKRT SITEYTRHGR GTKGMIAIQQ SERNGRVVAA TLVHADDEIM LITDTGVLVR
     TRVSEIRELG RATQGVTLIS LDEGAKLSGL QRIVENDANT AEADGADTAP AADDPH
//

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