ID A0A317V8C7_ASPEC Unreviewed; 747 AA.
AC A0A317V8C7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=AP endonuclease, family 2 {ECO:0000313|EMBL:PWY70623.1};
GN ORFNames=BO83DRAFT_363106 {ECO:0000313|EMBL:PWY70623.1};
OS Aspergillus eucalypticola (strain CBS 122712 / IBT 29274).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448314 {ECO:0000313|EMBL:PWY70623.1, ECO:0000313|Proteomes:UP000246171};
RN [1] {ECO:0000313|EMBL:PWY70623.1, ECO:0000313|Proteomes:UP000246171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 122712 {ECO:0000313|EMBL:PWY70623.1,
RC ECO:0000313|Proteomes:UP000246171};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: In the 2nd section; belongs to the type-I 3-dehydroquinase
CC family. {ECO:0000256|ARBA:ARBA00006477}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the shikimate kinase
CC family. {ECO:0000256|ARBA:ARBA00009349}.
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:PWY70623.1}.
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DR EMBL; MSFU01000016; PWY70623.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317V8C7; -.
DR VEuPathDB; FungiDB:BO83DRAFT_363106; -.
DR OrthoDB; 2256238at2759; -.
DR Proteomes; UP000246171; Unassembled WGS sequence.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:InterPro.
DR CDD; cd01065; NAD_bind_Shikimate_DH; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
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 Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR001381; DHquinase_I.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041121; SDH_C.
DR InterPro; IPR031322; Shikimate/glucono_kinase.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR022893; Shikimate_DH_fam.
DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR PANTHER; PTHR21089:SF1; BIFUNCTIONAL 3-DEHYDROQUINATE DEHYDRATASE_SHIKIMATE DEHYDROGENASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR21089; SHIKIMATE DEHYDROGENASE; 1.
DR Pfam; PF01487; DHquinase_I; 1.
DR Pfam; PF18317; SDH_C; 1.
DR Pfam; PF01488; Shikimate_DH; 1.
DR Pfam; PF08501; Shikimate_dh_N; 1.
DR Pfam; PF01202; SKI; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000313|EMBL:PWY70623.1};
KW Hydrolase {ECO:0000313|EMBL:PWY70623.1};
KW Nuclease {ECO:0000313|EMBL:PWY70623.1}.
FT DOMAIN 451..531
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 571..615
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 710..740
FT /note="SDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18317"
SQ SEQUENCE 747 AA; 82790 MW; 47BDDEC243F0F9D3 CRC64;
MSSLSSPLTP CDRLVSIPCR RYSADATLLL VGFVGAGKKT LGIIASVALR RRFIDFDAVF
RQEVHVSPQD YIAHNGSARY RELELKLTRS LLEKCSTGCV ITITGVGWSA NRQQQVLLKE
FAQNHPVVYV RRDRVDLQQF IMTTSPDKFN RIFEAGNEFF QSCSSFDFFN HTQEKVTDYA
GRPLPAYIKL KEAERVFLRF LHQVFGRAFH VLYSSDPFSP SHTYALQVPL TWLEDDPDLG
LLESGTDAVN LVIDGGAADV DDGRFMERIA KHMATIRKHT RVPISIEVPQ QSYPRCCELL
EMLFRLAPDV VACPIDSPNF SRLKLAKGHT KIIATYQSTS MTGNQSIFPE VRSLLEKIDE
IGFDAFRITS EPNFPGDLTN LYLQQRLGET TDIPVIAYHT GPLGRASICL NPILSPVILS
SPTEGDIGVT LASAQQALTS CYLLTKQTFT VFGQRVQNSL SPAMHNAAYT ACGLPHTYNI
LCSDRFSDIH QLLNSTEHGG VAVTLPYKTD VLTLLDEVSP DAQDIHAVNT VVIQRSNNPS
SKILKGYNTD YLGIRDCIYK HLSPANAIRH GTTALIIGAG GMARAAIFAC YQIGVRQMCI
YNRTSSNAQK LAGYYTRWAE KKDTSLQIEV LRSGNDPWPA GFRQPTIIVA CLPAPAGGQL
QAPVTMEVSE QWLRSTTGGV FIDVAYGMPQ TKLRMAMNER SSMGWVVVDG LVVLLEQGIA
QYELFTGRPA PVHVMRGVLR EYTNAVT
//
