(data stored in ACNUC7421 zone)

SWISSPROT: C3MFT8_SINFN

ID   C3MFT8_SINFN            Unreviewed;       101 AA.
AC   C3MFT8;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   08-MAY-2019, entry version 57.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ACP23989.1};
GN   OrderedLocusNames=NGR_c01890 {ECO:0000313|EMBL:ACP23989.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP23989.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP23989.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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DR   EMBL; CP001389; ACP23989.1; -; Genomic_DNA.
DR   RefSeq; WP_012706774.1; NC_012587.1.
DR   RefSeq; YP_002824742.1; NC_012587.1.
DR   STRING; 394.NGR_c01890; -.
DR   EnsemblBacteria; ACP23989; ACP23989; NGR_c01890.
DR   GeneID; 7790767; -.
DR   KEGG; rhi:NGR_c01890; -.
DR   PATRIC; fig|394.7.peg.2984; -.
DR   eggNOG; ENOG41084AM; Bacteria.
DR   eggNOG; COG1605; LUCA.
DR   HOGENOM; HOG000217291; -.
DR   KO; K04782; -.
DR   OMA; LIHWFIN; -.
DR   OrthoDB; 1980002at2; -.
DR   BioCyc; SFRE394:GBYN-188-MONOMER; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0016835; F:carbon-oxygen lyase activity; IEA:InterPro.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR   GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR   GO; GO:0009697; P:salicylic acid biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.20.59.10; -; 1.
DR   InterPro; IPR036263; Chorismate_II_sf.
DR   InterPro; IPR036979; CM_dom_sf.
DR   InterPro; IPR002701; CM_II_prokaryot.
DR   InterPro; IPR008241; Isochorismate_pyruvate-lyase.
DR   Pfam; PF01817; CM_2; 1.
DR   PIRSF; PIRSF029775; Isochor_pyr_lyas; 1.
DR   SMART; SM00830; CM_2; 1.
DR   SUPFAM; SSF48600; SSF48600; 1.
DR   TIGRFAMs; TIGR01803; CM-like; 1.
DR   PROSITE; PS51168; CHORISMATE_MUT_2; 1.
PE   4: Predicted;
DR   PRODOM; C3MFT8.
DR   SWISS-2DPAGE; C3MFT8.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   DOMAIN        5     96       Chorismate mutase. {ECO:0000259|PROSITE:
FT                                PS51168}.
FT   COILED       11     31       {ECO:0000256|SAM:Coils}.
FT   BINDING      15     15       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR029775-1}.
FT   BINDING      32     32       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR029775-1}.
FT   BINDING      43     43       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR029775-1}.
FT   BINDING      92     92       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR029775-1}.
SQ   SEQUENCE   101 AA;  11600 MW;  827CC34B20A25EE7 CRC64;
     MPKTPAECTT MADVRAEIDR LDRALMALFA ERWGYIDRAA EIKRPLNLKA DIPARVAEVR
     ENARRHAVAF GLEPDFYEEL WAQLIDHAIA HERTLLGEDQ E
//

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