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Database: UniProt
Entry: Q8NUQ5
LinkDB: Q8NUQ5
Original site: Q8NUQ5 
ID   CRTM_STAAW              Reviewed;         287 AA.
AC   Q8NUQ5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   19-FEB-2014, entry version 67.
DE   RecName: Full=Dehydrosqualene synthase;
DE            EC=2.5.1.96;
DE   AltName: Full=4,4'-diapophytoene synthase;
DE            Short=DAP synthase;
DE   AltName: Full=Diapophytoene synthase;
GN   Name=crtM; OrderedLocusNames=MW2483;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/S0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A.,
RA   Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L.,
RA   Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-
RT   acquired MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- FUNCTION: Catalyzes the head-to-head condensation of two molecules
CC       of farnesyl diphosphate (FPP) into the colorless C(30) carotenoid
CC       dehydrosqualene (4,4'-diapophytoene). This is the initial step in
CC       the biosynthesis of staphyloxanthin, an orange carotenoid present
CC       in most staphylococci strains (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2 (2E,6E)-farnesyl diphosphate = 4,4'-
CC       diapophytoene + 2 diphosphate.
CC   -!- PATHWAY: Carotenoid biosynthesis; staphyloxanthin biosynthesis;
CC       staphyloxanthin from farnesyl diphosphate: step 1/5.
CC   -!- SIMILARITY: Belongs to the phytoene/squalene synthase family. CrtM
CC       subfamily.
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DR   EMBL; BA000033; BAB96348.1; -; Genomic_DNA.
DR   RefSeq; NP_647300.1; NC_003923.1.
DR   ProteinModelPortal; Q8NUQ5; -.
DR   SMR; Q8NUQ5; 1-284.
DR   STRING; 196620.MW2483; -.
DR   EnsemblBacteria; BAB96348; BAB96348; BAB96348.
DR   GeneID; 1004619; -.
DR   KEGG; sam:MW2483; -.
DR   PATRIC; 19571710; VBIStaAur44266_2566.
DR   eggNOG; COG1562; -.
DR   HOGENOM; HOG000220848; -.
DR   KO; K10208; -.
DR   OMA; KRRAIWA; -.
DR   OrthoDB; EOG63FW00; -.
DR   ProtClustDB; CLSK886072; -.
DR   BioCyc; SAUR196620:GJ9Z-2559-MONOMER; -.
DR   UniPathway; UPA00029; UER00556.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.600.10; -; 1.
DR   InterPro; IPR002060; Squ/phyt_synthse.
DR   InterPro; IPR019845; Squalene/phytoene_synthase_CS.
DR   InterPro; IPR008949; Terpenoid_synth.
DR   Pfam; PF00494; SQS_PSY; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
DR   PROSITE; PS01044; SQUALEN_PHYTOEN_SYN_1; 1.
PE   3: Inferred from homology;
KW   Carotenoid biosynthesis; Complete proteome; Transferase.
FT   CHAIN         1    287       Dehydrosqualene synthase.
FT                                /FTId=PRO_0000282623.
FT   REGION       18     22       Farnesyl diphosphate 1 binding (By
FT                                similarity).
FT   REGION       45     48       Farnesyl diphosphate 2 binding (By
FT                                similarity).
FT   BINDING      41     41       Farnesyl diphosphate 1 (By similarity).
FT   BINDING     168    168       Farnesyl diphosphate 2 (By similarity).
FT   BINDING     171    171       Farnesyl diphosphate 1 (By similarity).
FT   BINDING     172    172       Farnesyl diphosphate 2 (By similarity).
FT   BINDING     248    248       Farnesyl diphosphate 1 (By similarity).
SQ   SEQUENCE   287 AA;  34231 MW;  2407009413D42E63 CRC64;
     MTMMDMNFKY CHKIMKKHSK SFSYAFDLLP EDQRKAVWAI YAVCRKIDDS IDVYGDIQFL
     NQIKEDIQSI EKYPYEHHHF QSDRRIMMAL QHVAQHKNIA FQSFYNLIDT VYKDQHFTMF
     ETDAELFGYC YGVAGTVGEV LTPILSDHET HQTYDVARRL GESLQLINIL RDVGEDFDNE
     RIYFSKQRLK QYEVDIAEVY QNGVNNHYID LWEYYAAIAE KDFQDVMDQI KVFSIEAQPI
     IELAARIYIE ILDEVRQANY TLHERVFVDK RKKAKLFHEI NSKYHRI
//
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