ID A0A1F7ZXR7_9EURO Unreviewed; 229 AA.
AC A0A1F7ZXR7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Shikimate / quinate 5-dehydrogenase {ECO:0000313|EMBL:OGM43838.1};
GN ORFNames=ABOM_007593 {ECO:0000313|EMBL:OGM43838.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM43838.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM43838.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
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:OGM43838.1}.
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DR EMBL; LYCR01000064; OGM43838.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7ZXR7; -.
DR STRING; 109264.A0A1F7ZXR7; -.
DR OrthoDB; 2456418at2759; -.
DR UniPathway; UPA00053; UER00087.
DR Proteomes; UP000179179; Unassembled WGS sequence.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR022893; Shikimate_DH_fam.
DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR PANTHER; PTHR21089:SF26; AROM POLYPEPTIDE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR21089; SHIKIMATE DEHYDROGENASE; 1.
DR Pfam; PF01488; Shikimate_DH; 1.
DR Pfam; PF08501; Shikimate_dh_N; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000179179}.
FT DOMAIN 11..91
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 131..183
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
SQ SEQUENCE 229 AA; 24519 MW; C93168BFC3A54ED4 CRC64;
MPTTTAQHYH IFGQGISQSL SPTIHNAAFA HYGLPHRYDI KECNSLQDVK PLIEDPAFGG
SSVTMPHKLS AGEFCAQVAD SATRLGAINT LIARFIDTED GTSKRQIHGD NTDWSGLYSL
IKEHATGEGK QVGLVIGAGG AARAGVYAMA QAGIERIYVG NRTLAKAEQI ARDFEDLCPV
IPVEFPSVLP EAPDVIIGTV PGDAMSQDAF KGLFGNEKGL CIEMAYKQE
//