ID A0A0N0NJD9_9EURO Unreviewed; 822 AA.
AC A0A0N0NJD9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Quinate repressor protein {ECO:0000313|EMBL:KPI36798.1};
GN ORFNames=AB675_11836 {ECO:0000313|EMBL:KPI36798.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI36798.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI36798.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI36798.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-2015) 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:KPI36798.1}.
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DR EMBL; LFJN01000028; KPI36798.1; -; Genomic_DNA.
DR RefSeq; XP_017996761.1; XM_018140716.1.
DR AlphaFoldDB; A0A0N0NJD9; -.
DR STRING; 1664694.A0A0N0NJD9; -.
DR GeneID; 28732597; -.
DR OrthoDB; 2256238at2759; -.
DR Proteomes; UP000038010; Unassembled WGS sequence.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:InterPro.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:InterPro.
DR CDD; cd00502; DHQase_I; 1.
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; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR PANTHER; PTHR21090; AROM/DEHYDROQUINATE SYNTHASE; 1.
DR PANTHER; PTHR21090:SF17; QUINATE REPRESSOR PROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000038010}.
FT DOMAIN 489..569
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 629..673
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 773..803
FT /note="SDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18317"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 822 AA; 89994 MW; 8E592B39445D18D9 CRC64;
MTRHSSEERA IRSAPSSPYI PNRTLALGHD GVRTSGQNTP SAATTNRTFH PDASVVLVGI
RGSGKRSLGL IAAAALGRRF ITEDHFFQLT TGFSRQDFLK NHGSELFHQS DVEVTRKMLE
ENKHHCVIDC GLGSMTSSLQ DYLRLYCMTN PVVYIMRDMV QIKSLLNLGD RSVKLLEAGD
PSHRKCSNFE YYNLQDDTAD EGSDETADRS SPTYSFKLRH AQEDFSRFVR QITNTAPNYS
STFSIDAPLE TRAYTHALEI PLSRLTDELD ISALEVAGDL VDIIIDKWNG HMSKVFSKAV
ASVRRHIGVP VCVTNRATEL GIDLRMAIIN HALRTGVEYV AIDLDRERNL IPSVLAMKGP
SRIIGTVQRR IPTGQDWRDH KLVELAQAAV SAKCDSVRII VPALSRNDLS SVLWLREELQ
SKLKPTVPVT IFASGSLGRA SQMLNTHMTS VTHPILKAGN DQFAPILTSA QLLQALGSSF
MLDALQFCIV GANVSQSLSP VMHNAAYEAT GLSHSYTLKN IISWDEVEAL AADDCFGGAS
VIQPWKVKAM EKVSSLSHHA RAIGAVNTLI PLRKDANGRM PPLATQAYNR NQAGPIAAWH
GDNTDFIGIK VCLSRSLSPR NVIQPKTTGL VVGAGGMARA AVYAMLQLGC KNVFIYNRTL
ANARAVASHF MSQSSRDGKA PSSAAGGLNV LVLENLEQAW PSGFAMPTMV VSCVTHERID
GNTEAVFKMP KQWLESPSGG VVVEMAYNHV TALVQQITQF RVETGIPWVV VPGVETLIEQ
AVAQFEIMVG RRGPRSVMTA AVKSVMNDKR YLTDFGSWRA SD
//
