ID A0A089YQY3_STRGA Unreviewed; 381 AA.
AC A0A089YQY3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Putative 3-dehydroquinate synthase {ECO:0000313|EMBL:AIR96070.1};
GN ORFNames=SGLAU_00210 {ECO:0000313|EMBL:AIR96070.1};
OS Streptomyces glaucescens.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1907 {ECO:0000313|EMBL:AIR96070.1, ECO:0000313|Proteomes:UP000029482};
RN [1] {ECO:0000313|Proteomes:UP000029482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40922 / GLA O {ECO:0000313|Proteomes:UP000029482};
RX PubMed=25499805; DOI=10.1016/j.jbiotec.2014.11.036;
RA Ortseifen V., Winkler A., Albersmeier A., Wendler S., Puhler A.,
RA Kalinowski J., Ruckert C.;
RT "Complete genome sequence of the actinobacterium Streptomyces glaucescens
RT GLA.O (DSM 40922) consisting of a linear chromosome and one linear
RT plasmid.";
RL J. Biotechnol. 194:81-83(2015).
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911};
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DR EMBL; CP009438; AIR96070.1; -; Genomic_DNA.
DR RefSeq; WP_043497242.1; NZ_CP009438.1.
DR AlphaFoldDB; A0A089YQY3; -.
DR STRING; 1907.SGLAU_00210; -.
DR KEGG; sgu:SGLAU_00210; -.
DR eggNOG; COG0337; Bacteria.
DR HOGENOM; CLU_001201_0_2_11; -.
DR OrthoDB; 9806583at2; -.
DR Proteomes; UP000029482; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:InterPro.
DR CDD; cd08195; DHQS; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR016037; DHQ_synth_AroB.
DR InterPro; IPR030963; DHQ_synth_fam.
DR InterPro; IPR030960; DHQS/DOIS.
DR NCBIfam; TIGR01357; aroB; 1.
DR PANTHER; PTHR43622; 3-DEHYDROQUINATE SYNTHASE; 1.
DR PANTHER; PTHR43622:SF1; 3-DEHYDROQUINATE SYNTHASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01761; DHQ_synthase; 1.
DR PIRSF; PIRSF001455; DHQ_synth; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE 4: Predicted;
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Lyase {ECO:0000256|ARBA:ARBA00023239}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000029482};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 118..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 88..336
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
SQ SEQUENCE 381 AA; 41356 MW; 021907C5DD3F6A1B CRC64;
MNLPEGTHVT HDAIPLPEPH HTIRARAQRR AEYAVALADS VEEAVKHLRT VVADQRIALV
TDDTVAALHA EELQAELHRQ DMDFTLASIP PGEESKTMRT AGSLLDWLAD SRMRRRDVLV
AFGGGVVIDT AGWVASAYMR GMPYVNLPTT LLAAVDAALG GKVAVDHPTA KNLIGAFHQP
TAVVAAVPWL STLPARHVRA GLAEAVKKGV IASPALFELI ERHLPDIQDL EPTTLRRLVH
GAATVKCALI DRDPYEEDLR RPLNFGHTIG HAVETVTGYG PVLHGEAVAF GMACAARISH
ARSWLDYASH TRFLTLLKRA GLPCERTQLP VPVDSEAVIT ALDKIRLIRD GRLRFVLPLG
IGTTAISDDV TDDEIRQALT S
//
