CRTM_STAAU
ID CRTM_STAAU Reviewed; 287 AA.
AC A9JQL9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=4,4'-diapophytoene synthase {ECO:0000250|UniProtKB:Q2FV59};
DE Short=DAP synthase {ECO:0000250|UniProtKB:Q2FV59};
DE EC=2.5.1.96 {ECO:0000269|PubMed:18276850};
DE AltName: Full=C30 carotenoid synthase {ECO:0000250|UniProtKB:Q2FV59};
DE AltName: Full=Dehydrosqualene synthase {ECO:0000303|PubMed:18276850};
GN Name=crtM {ECO:0000303|PubMed:18276850};
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS)
RP IN COMPLEXES WITH SUBSTRATE ANALOGS AND MAGNESIUM IONS, FUNCTION, CATALYTIC
RP ACTIVITY, AND COFACTOR.
RC STRAIN=ATCC 27659 / U9N0;
RX PubMed=18276850; DOI=10.1126/science.1153018;
RA Liu C.-I., Liu G.Y., Song Y., Yin F., Hensler M.E., Jeng W.-Y., Nizet V.,
RA Wang A.H.-J., Oldfield E.;
RT "A cholesterol biosynthesis inhibitor blocks Staphylococcus aureus
RT virulence.";
RL Science 319:1391-1394(2008).
CC -!- FUNCTION: Involved in the biosynthesis of the yellow-orange carotenoid
CC staphyloxanthin, which plays a role in the virulence via its protective
CC function against oxidative stress. Catalyzes the head-to-head
CC condensation of two molecules of farnesyl diphosphate (FPP) into the
CC colorless C(30) carotenoid 4,4'-diapophytoene (dehydrosqualene).
CC {ECO:0000269|PubMed:18276850}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (2E,6E)-farnesyl diphosphate = 15-cis-4,4'-diapophytoene + 2
CC diphosphate; Xref=Rhea:RHEA:31547, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:62738, ChEBI:CHEBI:175763; EC=2.5.1.96;
CC Evidence={ECO:0000269|PubMed:18276850};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18276850};
CC Note=Binds 2 Mg(2+) ions per subunit. A third Mg(2+) ion binds between
CC the 2 farnesyl diphosphate (FPP). {ECO:0000269|PubMed:18276850};
CC -!- PATHWAY: Carotenoid biosynthesis; staphyloxanthin biosynthesis;
CC staphyloxanthin from farnesyl diphosphate: step 1/5. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phytoene/squalene synthase family. CrtM
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM920687; CAP47341.1; -; Genomic_DNA.
DR RefSeq; WP_000178319.1; NZ_WKIS01000001.1.
DR PDB; 2ZCO; X-ray; 1.58 A; A=1-287.
DR PDB; 2ZCQ; X-ray; 2.38 A; A=1-287.
DR PDB; 2ZCR; X-ray; 1.92 A; A=1-287.
DR PDB; 2ZCS; X-ray; 2.03 A; A=1-287.
DR PDB; 2ZY1; X-ray; 1.78 A; A=1-287.
DR PDB; 3ACW; X-ray; 1.63 A; A=1-287.
DR PDB; 3ACX; X-ray; 1.31 A; A=1-287.
DR PDB; 3ACY; X-ray; 1.84 A; A=1-287.
DR PDB; 3ADZ; X-ray; 1.89 A; A=1-287.
DR PDB; 3AE0; X-ray; 2.37 A; A/B=1-287.
DR PDB; 3LGZ; X-ray; 2.41 A; B=1-287.
DR PDB; 3NPR; X-ray; 2.00 A; A=1-287.
DR PDB; 3TFN; X-ray; 2.07 A; A=1-287.
DR PDB; 3TFP; X-ray; 2.00 A; A=1-287.
DR PDB; 3TFV; X-ray; 3.00 A; A=1-287.
DR PDB; 3VJD; X-ray; 1.48 A; A=1-287.
DR PDB; 3VJE; X-ray; 2.12 A; A/B=1-287.
DR PDB; 3W7F; X-ray; 2.25 A; A/B=1-287.
DR PDB; 4E9U; X-ray; 2.10 A; A=1-287.
DR PDB; 4E9Z; X-ray; 2.06 A; A=1-287.
DR PDB; 4EA0; X-ray; 2.12 A; A/B=1-287.
DR PDB; 4EA1; X-ray; 2.46 A; A=1-287.
DR PDB; 4EA2; X-ray; 2.05 A; A=1-287.
DR PDB; 4F6V; X-ray; 2.30 A; A=1-287.
DR PDB; 4F6X; X-ray; 1.98 A; A=1-287.
DR PDBsum; 2ZCO; -.
DR PDBsum; 2ZCQ; -.
DR PDBsum; 2ZCR; -.
DR PDBsum; 2ZCS; -.
DR PDBsum; 2ZY1; -.
DR PDBsum; 3ACW; -.
DR PDBsum; 3ACX; -.
DR PDBsum; 3ACY; -.
DR PDBsum; 3ADZ; -.
DR PDBsum; 3AE0; -.
DR PDBsum; 3LGZ; -.
DR PDBsum; 3NPR; -.
DR PDBsum; 3TFN; -.
DR PDBsum; 3TFP; -.
DR PDBsum; 3TFV; -.
DR PDBsum; 3VJD; -.
DR PDBsum; 3VJE; -.
DR PDBsum; 3W7F; -.
DR PDBsum; 4E9U; -.
DR PDBsum; 4E9Z; -.
DR PDBsum; 4EA0; -.
DR PDBsum; 4EA1; -.
DR PDBsum; 4EA2; -.
DR PDBsum; 4F6V; -.
DR PDBsum; 4F6X; -.
DR AlphaFoldDB; A9JQL9; -.
DR SMR; A9JQL9; -.
DR BindingDB; A9JQL9; -.
DR ChEMBL; CHEMBL5440; -.
DR DrugBank; DB07420; (1R)-4-(3-phenoxyphenyl)-1-phosphonobutane-1-sulfonic acid.
DR DrugBank; DB04695; Farnesyl thiopyrophosphate.
DR DrugBank; DB07424; Tripotassium (1R)-4-biphenyl-4-yl-1-phosphonatobutane-1-sulfonate.
DR OMA; KLYCYRV; -.
DR BRENDA; 2.5.1.96; 3352.
DR UniPathway; UPA00029; UER00556.
DR EvolutionaryTrace; A9JQL9; -.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00683; Trans_IPPS_HH; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR002060; Squ/phyt_synthse.
DR InterPro; IPR019845; Squalene/phytoene_synthase_CS.
DR InterPro; IPR044843; Trans_IPPS_bact-type.
DR InterPro; IPR033904; Trans_IPPS_HH.
DR Pfam; PF00494; SQS_PSY; 1.
DR SFLD; SFLDG01212; Phytoene_synthase_like; 1.
DR SFLD; SFLDG01018; Squalene/Phytoene_Synthase_Lik; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR PROSITE; PS01044; SQUALEN_PHYTOEN_SYN_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carotenoid biosynthesis; Magnesium; Metal-binding;
KW Transferase; Virulence.
FT CHAIN 1..287
FT /note="4,4'-diapophytoene synthase"
FT /id="PRO_0000347335"
FT BINDING 18..21
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:18276850,
FT ECO:0007744|PDB:2ZCS, ECO:0007744|PDB:3W7F"
FT BINDING 41
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:18276850,
FT ECO:0007744|PDB:2ZCS, ECO:0007744|PDB:3W7F"
FT BINDING 45
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:18276850,
FT ECO:0007744|PDB:2ZCQ, ECO:0007744|PDB:3W7F"
FT BINDING 45
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:18276850,
FT ECO:0007744|PDB:2ZCQ, ECO:0007744|PDB:3W7F"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18276850,
FT ECO:0007744|PDB:2ZCQ, ECO:0007744|PDB:3W7F"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18276850,
FT ECO:0007744|PDB:2ZCQ, ECO:0007744|PDB:3W7F"
FT BINDING 165
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:18276850,
FT ECO:0007744|PDB:2ZCQ, ECO:0007744|PDB:2ZCR"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18276850,
FT ECO:0007744|PDB:2ZCQ, ECO:0007744|PDB:2ZCR,
FT ECO:0007744|PDB:3W7F"
FT BINDING 171
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:18276850,
FT ECO:0007744|PDB:3W7F"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18276850,
FT ECO:0007744|PDB:2ZCQ, ECO:0007744|PDB:2ZCR,
FT ECO:0007744|PDB:3W7F"
FT BINDING 248
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:18276850,
FT ECO:0007744|PDB:3W7F"
FT HELIX 3..18
FT /evidence="ECO:0007829|PDB:3ACX"
FT HELIX 20..26
FT /evidence="ECO:0007829|PDB:3ACX"
FT HELIX 31..49
FT /evidence="ECO:0007829|PDB:3ACX"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:3ACX"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:3VJD"
FT HELIX 58..72
FT /evidence="ECO:0007829|PDB:3ACX"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:3ACX"
FT HELIX 101..114
FT /evidence="ECO:0007829|PDB:3ACX"
FT HELIX 123..133
FT /evidence="ECO:0007829|PDB:3ACX"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:3ACX"
FT HELIX 151..171
FT /evidence="ECO:0007829|PDB:3ACX"
FT HELIX 173..178
FT /evidence="ECO:0007829|PDB:3ACX"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:3ACX"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:3ACX"
FT HELIX 206..228
FT /evidence="ECO:0007829|PDB:3ACX"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:3ACX"
FT HELIX 237..257
FT /evidence="ECO:0007829|PDB:3ACX"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:3ACX"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:3ACX"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:3ACX"
SQ SEQUENCE 287 AA; 34313 MW; 41AD734ABEB81214 CRC64;
MTMMDMNFKY CHKIMKKHSK SFSYAFDLLP EDQRKAVWAI YAVCRKIDDS IDVYGDIQFL
NQIKEDIQSI EKYPYEYHHF QSDRRIMMAL QHVAQHKNIA FQSFYNLIDT VYKDQHFTMF
ETDAELFGYC YGVAGTVGEV LTPILSDHET HQTYDVARRL GESLQLINIL RDVGEDFENE
RIYFSKQRLK QYEVDIAEVY QNGVNNHYID LWEYYAAIAE KDFRDVMDQI KVFSIEAQPI
IELAARIYIE ILDEVRQANY TLHERVFVEK RKKAKLFHEI NSKYHRI
