(data stored in SCRATCH zone)

SWISSPROT: C1ARS9_RHOOB

ID   C1ARS9_RHOOB            Unreviewed;       650 AA.
AC   C1ARS9;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 50.
DE   SubName: Full=Putative 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000313|EMBL:BAH48756.1};
DE            EC=3.7.1.- {ECO:0000313|EMBL:BAH48756.1};
GN   OrderedLocusNames=ROP_05090 {ECO:0000313|EMBL:BAH48756.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48756.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48756.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48756.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; AP011115; BAH48756.1; -; Genomic_DNA.
DR   RefSeq; WP_012687763.1; NC_012522.1.
DR   ProteinModelPortal; C1ARS9; -.
DR   STRING; 632772.ROP_05090; -.
DR   EnsemblBacteria; BAH48756; BAH48756; ROP_05090.
DR   KEGG; rop:ROP_05090; -.
DR   PATRIC; fig|632772.20.peg.562; -.
DR   eggNOG; ENOG4107QK6; Bacteria.
DR   eggNOG; COG3962; LUCA.
DR   HOGENOM; HOG000239708; -.
DR   KO; K03336; -.
DR   OMA; FEDHANG; -.
DR   OrthoDB; POG091H02KO; -.
DR   BioCyc; ROPA632772:GH0Q-508-MONOMER; -.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0016823; F:hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0019310; P:inositol catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1220; -; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR030817; Myo_inos_iolD.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   PANTHER; PTHR18968:SF140; PTHR18968:SF140; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR04377; myo_inos_iolD; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1ARS9.
DR   SWISS-2DPAGE; C1ARS9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   Hydrolase {ECO:0000313|EMBL:BAH48756.1};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN       13    202       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      225    359       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      435    604       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   650 AA;  69875 MW;  E672BB0A84B75C59 CRC64;
     MTPLSTHKTI RLTTAQAVVK YLAAQYSVAD GERRRLIPAA LGIFGHGNVA GLGQALDELS
     DDLPFIQGRH EQYLAHIATA YAKASRRRAT LAVTASIGPG ALNLVTAAGL ATINRLPLLL
     LPGDTYATRH QGPVLQQLEH ASEADLTVND TFRPVAKFFD RITRPEQLLT ALPQAMRVLT
     SPTDTGAVVL SLPQDVQSHA FDFPIEFFEP RDWRIRRPLP DPAEVEAVAA QIREASRPVI
     IAGGGVHYSD ATAALEALAE QAGIPVVESF GGKGAVSRDE WWQVGGIGLE GNFASNKLVK
     QADLVLSVGT RLTDFVTGSQ SIFENENVRF AALNVVDADT RKQGATGILA DARLGLEALT
     TALAGHTTSD TWQQTVRSAK ADWAPIRAAA LDPDTAFEPA QHPHAPVTGA VLTQPQLIGL
     MQEHARSGDT IIAAAGGPPG DLQKVWDATG NRNVHLEFGF SCMGYEIPAA MGVRLAEGNR
     GQRIVTFIGD GTYLMAPTEL VTAAQEGLDV TIVVSENHGY QVIHRLQMNR NGREFGNEFR
     YRTDGDIIAD GGDKARLEGE YLKVDLRQIA EGLGATAIRA TTAADVRAAL IETREVSGPV
     VIVVPTVPHV DLPGGDVWWD VAPAEVSNQE WVQTLRADYD NAVGRQRWFG
//

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