ID A0A3L8SCZ7_CHLGU Unreviewed; 507 AA.
AC A0A3L8SCZ7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=3-dehydroquinate synthase domain-containing protein {ECO:0000259|Pfam:PF01761};
GN ORFNames=DV515_00009575 {ECO:0000313|EMBL:RLV99677.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV99677.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLV99677.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLV99677.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLV99677.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLV99677.1}.
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; QUSF01000031; RLV99677.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8SCZ7; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR CDD; cd08199; EEVS; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR030960; DHQS/DOIS.
DR InterPro; IPR035872; EEVS-like.
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 SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000276834}.
FT DOMAIN 206..308
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
FT REGION 26..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 507 AA; 56449 MW; 48B57B005E5B8561 CRC64;
MDWLWEASGA SSGSIRGIQR PEVVCSRAGQ KGRPLKSTSK APSDGRSLGR EISPSGSMLV
TEEACAAAVP GATMPQEPQQ TDFQLVRVRS TWCRIKKGEA LSNDEDEITL SEAKIGERIS
EGGISWIIEA PIYFCYKVVE TYNILEPSNT TLLWGHITDP QQIELATASK RKLRRFIVID
EVVDKLYGSK VREYFEENNV QHKILALPTT EETKSMDLVL NILHEVQNFS LDRRTEPIIA
IGGGVCLDIV GLAASLYRRR TPYIRVPTTL LSYVDASVGA KNGVNFLQCK NKLGGYTPPM
ALMKHKGLFD LLKSHGKYLL DTKFQSCNSF AHHGDAALQT TRIAIETMLE ELAPNLWEDD
LDRLVDFGHL ISPELEMRVL PSLMHGEAVN VDMAFMTYVA HARGLLGAEE KEQILQCMRG
LELPVWHSGC SWALIQRALR ERLKHGGGQP RMPLPTGLGV ADIFNDTSEE TLERAYKLWV
KDCKMELEEE LQAQGDGPAR SLSCLPL
//
