(data stored in SCRATCH3701 zone)

HOGENOM6: ACHXA_1_PE1685

ID   ACHXA_1_PE1685                       STANDARD;      PRT;   889 AA.
AC   ACHXA_1_PE1685; E3HVP4;
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; (ACHXA_1.PE1685).
GN   Name=gyrA; OrderedLocusNames=AXYL_01710;
OS   ACHROMOBACTER XYLOSOXIDANS A8.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=762376;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACHXA_1.PE1685.
CC       Achromobacter xylosoxidans A8 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:E3HVP4_ACHXA
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; E3HVP4; -.
DR   EMBL; CP002287; ADP15047.1; -; Genomic_DNA.
DR   RefSeq; YP_003977762.1; NC_014640.1.
DR   GeneID; 9896042; -.
DR   GenomeReviews; CP002287_GR; AXYL_01710.
DR   KEGG; axy:AXYL_01710; -.
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; ACHXA_1.PE1685; -.
DR   PRODOM; ACHXA_1_PE1685.
DR   SWISS-2DPAGE; ACHXA_1_PE1685.
KW   DNA gyrase subunit A;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   889 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDSFAKETLP VSLEEEMRRS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY AMHELNNDWN
     RAYKKSARIV GDVIGKYHPH GDQSVYDTIV RMAQDFSMRY MLVDGQGNFG SIDGDNAAAM
     RYTEIRLAKI AHELLADIDQ ETVDFGPNYD GSEQEPLLLP SRLPNLLVNG SSGIAVGMAT
     NIPPHNLQEV VDGCLYCLRN PGCSVDELME LIPAPDFPTG GIIYGMSGVR EGYRTGRGRV
     IMRAKTHFED MEKGNRQAIV VDAIPYQVNK KTLQERIAEL VNDKKIEGIS DIRDESDKDG
     MRLVIELKRG EVPEVVLNNL YKNTQLQDTF GMNLVALVDG QPRLLNLKQM IDYFLQHRRE
     VVTRRTVFQL RKARERGHVL EGLAVALANI DDFIAIIKAA PTPPVARQEL MAKSWDSSLV
     REMLSRADGD TPGGRAAFRP DDLGTEFGLQ GDGMYRLSDT QAQEILNMRL QRLTGLEQDK
     IVGEYKDIMS TIADLLDILA RPERITTIIS DELQAIKAEF STGVKDTRRS DIELNATELD
     TEDLITPTDM VVTLSHGGYI KSQPLSEYRS QKRGGRGKQA TAMKENDWID QLFIANTHDF
     LLCFSNRGRV YWLKVWEVPQ GTRNSRGKPI VNMFPLTEGE KITVVLPVKE FSEDHYVFMA
     TSRGTVKKTP LSDFSNPRKA GIIAVDLDDG DYLIGADLTD GKHDVMLFSD AGKAVRFDEN
     DVRPMGRNAR GVRGMMLEDT QTVIALLVAG DETQSVLTAT ENGYGKRTPI TEYTRHGRGT
     KGMIAIQTSS RNGKVVGAVL VMPSDEIMLI TTGGVLVRTR VSEIREMGRA TQGVTLINVD
     DGSSLSGVRR VVESDADDDG DLGEDGQEAD GGDDNGAADS TDSTEPTEQ
//

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