(data stored in ACNUC7421 zone)

SWISSPROT: C7QJ63_CATAD

ID   C7QJ63_CATAD            Unreviewed;       417 AA.
AC   C7QJ63;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 49.
DE   SubName: Full=Amidase, hydantoinase/carbamoylase family {ECO:0000313|EMBL:ACU69205.1};
DE            EC=3.5.1.87 {ECO:0000313|EMBL:ACU69205.1};
GN   OrderedLocusNames=Caci_0252 {ECO:0000313|EMBL:ACU69205.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69205.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69205.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
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DR   EMBL; CP001700; ACU69205.1; -; Genomic_DNA.
DR   ProteinModelPortal; C7QJ63; -.
DR   STRING; 479433.Caci_0252; -.
DR   EnsemblBacteria; ACU69205; ACU69205; Caci_0252.
DR   KEGG; cai:Caci_0252; -.
DR   eggNOG; ENOG4105CE7; Bacteria.
DR   eggNOG; COG0624; LUCA.
DR   HOGENOM; HOG000241291; -.
DR   KO; K06016; -.
DR   OMA; IWPHGRW; -.
DR   OrthoDB; POG091H0MM7; -.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR   GO; GO:0050538; F:N-carbamoyl-L-amino-acid hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   CDD; cd03884; M20_bAS; 1.
DR   InterPro; IPR010158; Amidase_Cbmase.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF001235; Amidase_carbamoylase; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
DR   TIGRFAMs; TIGR01879; hydantase; 1.
PE   4: Predicted;
DR   PRODOM; C7QJ63.
DR   SWISS-2DPAGE; C7QJ63.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Hydrolase {ECO:0000313|EMBL:ACU69205.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851}.
SQ   SEQUENCE   417 AA;  44265 MW;  1DB565CC2D6E013E CRC64;
     MSLFSVHRAV DEAEASAYSD MWRSLLPLGL NSDTGGYRRF AWNTADLACR DWFRSEAAAR
     GLEVETDRNG NLWAWWGPKG PGAIVTGSHL DSVPDGGAFD GPLGVVSSFA AVDVLRARGF
     TPAKPFAVAC FSDEEGARFG IACAGSRLMT GALSAEKARG LCDLDGVTMA SAMEQAGQDP
     ATLGRDDERL EGIAAYVELH VEQGKALAFT ESPVAVASAI WPHSRWRFEF AGEANHAGTT
     RLEDRRDPML TYANAVLAAR KKAKLGGAVA TFGRLVVEPN GTNAIPSRVR AWLDVRAPAD
     EILAAVTEEI IKAADERAGR DGTVLSTERE SHTPVVEFDD VLRNRLAGSL RQTFGAVPVL
     PTGAGHDAGI LAAAVPTAML YVRNPTGVSH APGEHADDRD CLAGVTALAD VLQELCQ
//

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