CRTM_STAAS
ID CRTM_STAAS Reviewed; 287 AA.
AC Q6G6B2;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
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:0000250|UniProtKB:Q2FV59};
DE AltName: Full=C30 carotenoid synthase {ECO:0000250|UniProtKB:Q2FV59};
DE AltName: Full=Dehydrosqualene synthase {ECO:0000250|UniProtKB:Q2FV59};
GN Name=crtM; OrderedLocusNames=SAS2448;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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:0000250|UniProtKB:Q2FV59}.
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:0000250|UniProtKB:Q2FV59};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A9JQL9};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:A9JQL9};
CC -!- PATHWAY: Carotenoid biosynthesis; staphyloxanthin biosynthesis;
CC staphyloxanthin from farnesyl diphosphate: step 1/5.
CC {ECO:0000250|UniProtKB:Q2FV59}.
CC -!- SIMILARITY: Belongs to the phytoene/squalene synthase family. CrtM
CC subfamily. {ECO:0000305}.
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DR EMBL; BX571857; CAG44264.1; -; Genomic_DNA.
DR RefSeq; WP_000178307.1; NC_002953.3.
DR AlphaFoldDB; Q6G6B2; -.
DR SMR; Q6G6B2; -.
DR KEGG; sas:SAS2448; -.
DR HOGENOM; CLU_037269_1_3_9; -.
DR OMA; KLYCYRV; -.
DR UniPathway; UPA00029; UER00556.
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 3: Inferred from homology;
KW Carotenoid biosynthesis; Magnesium; Metal-binding; Transferase; Virulence.
FT CHAIN 1..287
FT /note="4,4'-diapophytoene synthase"
FT /id="PRO_0000282622"
FT BINDING 18..21
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A9JQL9"
FT BINDING 41
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A9JQL9"
FT BINDING 45
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A9JQL9"
FT BINDING 45
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A9JQL9"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A9JQL9"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A9JQL9"
FT BINDING 165
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A9JQL9"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A9JQL9"
FT BINDING 171
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A9JQL9"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A9JQL9"
FT BINDING 248
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A9JQL9"
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
