CRTM_STAA3
ID CRTM_STAA3 Reviewed; 287 AA.
AC Q2FDU5;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=SAUSA300_2499;
OS Staphylococcus aureus (strain USA300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=367830;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USA300;
RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA Perdreau-Remington F.;
RT "Complete genome sequence of USA300, an epidemic clone of community-
RT acquired meticillin-resistant Staphylococcus aureus.";
RL Lancet 367:731-739(2006).
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; CP000255; ABD21608.1; -; Genomic_DNA.
DR RefSeq; WP_000178307.1; NZ_CP027476.1.
DR AlphaFoldDB; Q2FDU5; -.
DR SMR; Q2FDU5; -.
DR PRIDE; Q2FDU5; -.
DR EnsemblBacteria; ABD21608; ABD21608; SAUSA300_2499.
DR KEGG; saa:SAUSA300_2499; -.
DR HOGENOM; CLU_037269_1_3_9; -.
DR OMA; KLYCYRV; -.
DR UniPathway; UPA00029; UER00556.
DR Proteomes; UP000001939; Chromosome.
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_0000282617"
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
