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 02-SEP-2026, entry version 82. 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; Bacillati; Bacillota; Bacilli; Caryophanales; 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; NC_021670.1. 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 AlphaFoldDB; A9JQL9; -. DR MDposit; A9JQL9; -. DR MDRepo; 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:geranylgeranyl diphosphate synthase activity; IEA:InterPro. DR GO; GO:0051996; F:squalene synthase [NAD(P)H] activity; IEA:InterPro. DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-ARBA. DR CDD; cd00683; Trans_IPPS_HH; 1. DR FunFam; 1.10.600.10:FF:000028; Dehydrosqualene synthase; 1. DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 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 PANTHER; PTHR31480; BIFUNCTIONAL LYCOPENE CYCLASE/PHYTOENE SYNTHASE; 1. DR Pfam; PF00494; SQS_PSY; 1. DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1. DR SFLD; SFLDG01212; Phytoene_synthase_like; 1. DR SFLD; SFLDG01018; Squalene/Phytoene_Synthase_Lik; 1. DR SUPFAM; SSF48576; Terpenoid synthases; 1. DR PROSITE; PS01044; SQUALEN_PHYTOEN_SYN_1; 1. 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; -. 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 118..120 FT /evidence="ECO:0007829|PDB:3VJD" FT HELIX 123..130 FT /evidence="ECO:0007829|PDB:3ACX" FT HELIX 131..135 FT /evidence="ECO:0007829|PDB:3ACX" FT HELIX 136..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 230..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 //