ID A0A0F7PET6_9EURY Unreviewed; 384 AA.
AC A0A0F7PET6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Chorismate synthase {ECO:0000256|ARBA:ARBA00013036, ECO:0000256|HAMAP-Rule:MF_00300};
DE Short=CS {ECO:0000256|HAMAP-Rule:MF_00300};
DE EC=4.2.3.5 {ECO:0000256|ARBA:ARBA00013036, ECO:0000256|HAMAP-Rule:MF_00300};
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase {ECO:0000256|HAMAP-Rule:MF_00300};
GN Name=aroC {ECO:0000256|HAMAP-Rule:MF_00300,
GN ECO:0000313|EMBL:AKH98114.1};
GN ORFNames=HLASA_1625 {ECO:0000313|EMBL:ALG82508.1}, HLASF_1638
GN {ECO:0000313|EMBL:AKH98114.1};
OS Halanaeroarchaeum sulfurireducens.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halanaeroarchaeum.
OX NCBI_TaxID=1604004 {ECO:0000313|EMBL:AKH98114.1, ECO:0000313|Proteomes:UP000069906};
RN [1] {ECO:0000313|EMBL:AKH98114.1, ECO:0000313|Proteomes:UP000069906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HSR2 {ECO:0000313|EMBL:AKH98114.1,
RC ECO:0000313|Proteomes:UP000069906};
RX PubMed=25978546;
RA Sorokin D.Y., Kublanov I.V., Gavrilov S.N., Rojo D., Roman P.,
RA Golyshin P.N., Slepak V.Z., Smedile F., Ferrer M., Messina E., La Cono V.,
RA Yakimov M.M.;
RT "Elemental sulfur and acetate can support life of a novel strictly
RT anaerobic haloarchaeon.";
RL ISME J. 0:0-0(2015).
RN [2] {ECO:0000313|Proteomes:UP000060390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M27-SA2 {ECO:0000313|Proteomes:UP000060390};
RA Messina E., Kublanov I.V., Toshchakov S., Arcadi E., La Spada G.,
RA La Cono V., Yakimov M.M.;
RT "Complete genome sequence of Halanaeroarchaeum sulfurireducens type strain
RT M27-SA2, a sulfate-reducer haloarchaeon from marine anoxic lake Medee.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ALG82508.1, ECO:0000313|Proteomes:UP000060390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M27-SA2 {ECO:0000313|EMBL:ALG82508.1,
RC ECO:0000313|Proteomes:UP000060390};
RX PubMed=27182430; DOI=10.1186/s40793-016-0155-9;
RA Messina E., Sorokin D.Y., Kublanov I.V., Toshchakov S., Lopatina A.,
RA Arcadi E., Smedile F., La Spada G., La Cono V., Yakimov M.M.;
RT "Complete genome sequence of 'Halanaeroarchaeum sulfurireducens' M27-SA2, a
RT sulfur-reducing and acetate-oxidizing haloarchaeon from the deep-sea
RT hypersaline anoxic lake Medee.";
RL Stand. Genomic Sci. 11:35-35(2016).
CC -!- FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and
CC the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to
CC yield chorismate, which is the branch point compound that serves as the
CC starting substrate for the three terminal pathways of aromatic amino
CC acid biosynthesis. This reaction introduces a second double bond into
CC the aromatic ring system. {ECO:0000256|HAMAP-Rule:MF_00300}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate +
CC phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00300,
CC ECO:0000256|RuleBase:RU000605};
CC -!- COFACTOR:
CC Name=FMNH2; Xref=ChEBI:CHEBI:57618;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00300,
CC ECO:0000256|RuleBase:RU000605};
CC Note=Reduced FMN (FMNH(2)). {ECO:0000256|HAMAP-Rule:MF_00300,
CC ECO:0000256|RuleBase:RU000605};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 7/7. {ECO:0000256|ARBA:ARBA00005044, ECO:0000256|HAMAP-Rule:MF_00300,
CC ECO:0000256|RuleBase:RU000605}.
CC -!- SIMILARITY: Belongs to the chorismate synthase family.
CC {ECO:0000256|ARBA:ARBA00008014, ECO:0000256|HAMAP-Rule:MF_00300,
CC ECO:0000256|RuleBase:RU000605}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00300}.
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DR EMBL; CP008874; AKH98114.1; -; Genomic_DNA.
DR EMBL; CP011564; ALG82508.1; -; Genomic_DNA.
DR RefSeq; WP_050048801.1; NZ_CP011564.1.
DR AlphaFoldDB; A0A0F7PET6; -.
DR STRING; 1604004.HLASA_1625; -.
DR GeneID; 26010961; -.
DR KEGG; hsf:HLASA_1625; -.
DR KEGG; hsu:HLASF_1638; -.
DR PATRIC; fig|1604004.4.peg.1713; -.
DR HOGENOM; CLU_034547_0_0_2; -.
DR OrthoDB; 33049at2157; -.
DR UniPathway; UPA00053; UER00090.
DR Proteomes; UP000060390; Chromosome.
DR Proteomes; UP000069906; Chromosome.
DR GO; GO:0004107; F:chorismate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07304; Chorismate_synthase; 1.
DR Gene3D; 3.60.150.10; Chorismate synthase AroC; 1.
DR HAMAP; MF_00300; Chorismate_synth; 1.
DR InterPro; IPR000453; Chorismate_synth.
DR InterPro; IPR035904; Chorismate_synth_AroC_sf.
DR InterPro; IPR020541; Chorismate_synthase_CS.
DR NCBIfam; TIGR00033; aroC; 1.
DR PANTHER; PTHR21085; CHORISMATE SYNTHASE; 1.
DR PANTHER; PTHR21085:SF0; CHORISMATE SYNTHASE; 1.
DR Pfam; PF01264; Chorismate_synt; 1.
DR PIRSF; PIRSF001456; Chorismate_synth; 1.
DR SUPFAM; SSF103263; Chorismate synthase, AroC; 1.
DR PROSITE; PS00787; CHORISMATE_SYNTHASE_1; 1.
DR PROSITE; PS00788; CHORISMATE_SYNTHASE_2; 1.
DR PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00300};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_00300}; FAD {ECO:0000256|HAMAP-Rule:MF_00300};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00300};
KW FMN {ECO:0000256|HAMAP-Rule:MF_00300};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00300};
KW NADP {ECO:0000256|HAMAP-Rule:MF_00300};
KW Reference proteome {ECO:0000313|Proteomes:UP000069906}.
FT REGION 259..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT BINDING 125..127
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT BINDING 286
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT BINDING 301..305
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT BINDING 328
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
SQ SEQUENCE 384 AA; 41614 MW; F04786523E12B9F6 CRC64;
MNGNRFGRLF QVTTYGESHG PGMGVVVSGV PAGLDLSAAD VQHELDRRKP GQSTMTTSRD
EPDAVTIESG LQDGVTTGTP IGMTIQNRDA QSEKYEPFVT APRPSHGDFT YSAKFGTRNW
GGGGRSSARE TANWVAAGAI ATKVLASQGI EIAAHVNQID DIRAPPVDFE QIEAHTDDNE
VRCAHPETAE RMRERVEEYQ REGDSIGGSV YFEARGVPRG LGAPRFESVE ARLGQGMMAI
PASTAFEFGL GREAREYTGS ERNDEWGFDD AGDPTPVEND HGGVQGGITT GEPIYGEVTL
HAPTSIPKEQ ETVDWETGEP KTVQVTGRHD PVLPPRAVPV VESVLALTLV DFMLLSGRIN
PDRLDGQVGE YDTDYHPENP RRNE
//
