CRTM_STAAE
ID CRTM_STAAE Reviewed; 287 AA.
AC O07854; A6QK52; Q53722;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 110.
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:8002598};
DE AltName: Full=C30 carotenoid synthase {ECO:0000250|UniProtKB:Q2FV59};
DE AltName: Full=Dehydrosqualene synthase {ECO:0000303|PubMed:8002598};
GN Name=crtM {ECO:0000303|PubMed:8002598}; OrderedLocusNames=NWMN_2462;
OS Staphylococcus aureus (strain Newman).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=426430;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=Newman;
RX PubMed=8002598; DOI=10.1128/jb.176.24.7719-7726.1994;
RA Wieland B., Feil C., Gloria-Maercker E., Thumm G., Lechner M., Bravo J.-M.,
RA Poralla K., Goetz F.;
RT "Genetic and biochemical analyses of the biosynthesis of the yellow
RT carotenoid 4,4'-diaponeurosporene of Staphylococcus aureus.";
RL J. Bacteriol. 176:7719-7726(1994).
RN [2]
RP SEQUENCE REVISION.
RA Wieland B.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Newman;
RX PubMed=17951380; DOI=10.1128/jb.01000-07;
RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT analysis of staphylococcal genomes: polymorphism and evolution of two major
RT pathogenicity islands.";
RL J. Bacteriol. 190:300-310(2008).
RN [4]
RP SUBSTRATE SPECIFICITY, AND PATHWAY.
RX PubMed=11566453; DOI=10.1016/s1388-1981(01)00154-8;
RA Raisig A., Sandmann G.;
RT "Functional properties of diapophytoene and related desaturases of C(30)
RT and C(40) carotenoid biosynthetic pathways.";
RL Biochim. Biophys. Acta 1533:164-170(2001).
RN [5]
RP PATHWAY.
RX PubMed=16020541; DOI=10.1074/jbc.m505070200;
RA Pelz A., Wieland K.-P., Putzbach K., Hentschel P., Albert K., Goetz F.;
RT "Structure and biosynthesis of staphyloxanthin from Staphylococcus
RT aureus.";
RL J. Biol. Chem. 280:32493-32498(2005).
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:8002598}.
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:8002598};
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:0000269|PubMed:16020541, ECO:0000305|PubMed:11566453,
CC ECO:0000305|PubMed:8002598}.
CC -!- MISCELLANEOUS: Upon coexpression with Rhodobacter
CC geranylgeranyldiphosphate (GGDP) synthase, CrtM produces very small
CC amounts of C(40) phytoene. {ECO:0000269|PubMed:11566453}.
CC -!- SIMILARITY: Belongs to the phytoene/squalene synthase family. CrtM
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA52097.1; Type=Frameshift; Evidence={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; X73889; CAA52097.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AP009351; BAF68734.1; -; Genomic_DNA.
DR PIR; A55548; A55548.
DR RefSeq; WP_000178307.1; NZ_CP023390.1.
DR AlphaFoldDB; O07854; -.
DR SMR; O07854; -.
DR EnsemblBacteria; BAF68734; BAF68734; NWMN_2462.
DR KEGG; sae:NWMN_2462; -.
DR HOGENOM; CLU_037269_1_3_9; -.
DR OMA; KLYCYRV; -.
DR BioCyc; MetaCyc:MON-13873; -.
DR BRENDA; 2.5.1.96; 3352.
DR UniPathway; UPA00029; UER00556.
DR Proteomes; UP000006386; 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 1: Evidence at protein level;
KW Carotenoid biosynthesis; Magnesium; Metal-binding; Transferase; Virulence.
FT CHAIN 1..287
FT /note="4,4'-diapophytoene synthase"
FT /id="PRO_0000282615"
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"
FT CONFLICT 61
FT /note="N -> I (in Ref. 1; CAA52097)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="Q -> S (in Ref. 1; CAA52097)"
FT /evidence="ECO:0000305"
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
