(data stored in ACNUC7421 zone)

SWISSPROT: D6ZB28_SEGRD

ID   D6ZB28_SEGRD            Unreviewed;       419 AA.
AC   D6ZB28;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 49.
DE   SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:ADG96787.1};
GN   OrderedLocusNames=Srot_0300 {ECO:0000313|EMBL:ADG96787.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96787.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96787.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
CC   -!- SIMILARITY: Belongs to the beta-ketoacyl-ACP synthases family.
CC       {ECO:0000256|RuleBase:RU003694, ECO:0000256|SAAS:SAAS01172730}.
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DR   EMBL; CP001958; ADG96787.1; -; Genomic_DNA.
DR   RefSeq; WP_013137243.1; NC_014168.1.
DR   STRING; 640132.Srot_0300; -.
DR   EnsemblBacteria; ADG96787; ADG96787; Srot_0300.
DR   KEGG; srt:Srot_0300; -.
DR   eggNOG; ENOG4105C0Q; Bacteria.
DR   eggNOG; COG0304; LUCA.
DR   HOGENOM; HOG000060166; -.
DR   KO; K11609; -.
DR   OMA; FGSDIDN; -.
DR   OrthoDB; 606297at2; -.
DR   BioCyc; SROT640132:G1GLH-302-MONOMER; -.
DR   Proteomes; UP000002247; Chromosome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR000794; Beta-ketoacyl_synthase.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR11712; PTHR11712; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF53901; SSF53901; 2.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6ZB28.
DR   SWISS-2DPAGE; D6ZB28.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247};
KW   Transferase {ECO:0000256|RuleBase:RU003694,
KW   ECO:0000256|SAAS:SAAS01184688}.
FT   DOMAIN       14    410       PKS_KS. {ECO:0000259|SMART:SM00825}.
SQ   SEQUENCE   419 AA;  43584 MW;  E5684814358891DE CRC64;
     MARPSTANGG FPSIVVTGMA MMSAIAPDVE GTWQGLLDGE SGIRALEDDF AAGLDLPVRI
     GGRLKVRDFD KDLTKVEHRR MSYVQRMATV LGRQAWADAG SPDGVDEARL AVAIGAGMGS
     VRGMAEAYDE MREKGARAIS PFTVQMFMAN GPAAVVGLER KARGGIITPV SACASGNEAI
     AHAWRQIAYG DADIAICGGV EAAIDAFAVA AFANMRIVLS TANDEPEKAS RPFDKNRTGF
     VFGESGALLV IETEEHAKAR GARSYARLLG AGITSDGHHL VAPHPDGVGA ARAMTRALEN
     AGLQPGDVGH VNAHATATSV GDLAEAKAIR LAGLQHAEVY APKGAIGHSV GAVGAVEAVI
     TVKTLQEGII PPTLNLETPD PEIDLDVVSG EPRKSDHAYA INNSFGFGGH NTATVFGKY
//

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