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Database: UniProt
Entry: A0A093VF37_TALMA
LinkDB: A0A093VF37_TALMA
Original site: A0A093VF37_TALMA 
ID   A0A093VF37_TALMA        Unreviewed;       805 AA.
AC   A0A093VF37;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Quinate repressor protein {ECO:0000313|EMBL:KFX45311.1};
GN   ORFNames=GQ26_0241410 {ECO:0000313|EMBL:KFX45311.1};
OS   Talaromyces marneffei PM1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX45311.1, ECO:0000313|Proteomes:UP000029285};
RN   [1] {ECO:0000313|EMBL:KFX45311.1, ECO:0000313|Proteomes:UP000029285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PM1 {ECO:0000313|EMBL:KFX45311.1,
RC   ECO:0000313|Proteomes:UP000029285};
RX   PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA   Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA   Lin X.;
RT   "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT   of Dimorphic Transition in Penicillium marneffei.";
RL   PLoS Genet. 10:e1004662-e1004662(2014).
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:KFX45311.1}.
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DR   EMBL; JPOX01000024; KFX45311.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093VF37; -.
DR   eggNOG; KOG0692; Eukaryota.
DR   HOGENOM; CLU_008871_0_1_1; -.
DR   Proteomes; UP000029285; Unassembled WGS sequence.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase 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; 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; PF01202; SKI; 1.
DR   PRINTS; PR01100; SHIKIMTKNASE.
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;
FT   DOMAIN          612..655
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   DOMAIN          751..781
FT                   /note="SDH C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18317"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   805 AA;  89489 MW;  6CEDDDC43E1B8544 CRC64;
     MSPMVPAKKP PSKVHMLGTP ASKRNFAPDA SLVLVGIRGS GKRSLGFIAA AALNRRFITE
     DYYFKEVTGL TRHEFLLKFG SHEFQRRDVE VLKMMLDNHR THCVIECGLG SLTRIIQEHL
     RQYALTNPVV YLLRDMDQIQ RLLQLQDFSV KRLGNGDPYH RTCSNFEYYN LEEPVPVDLS
     LEEGAPDRRS VNYSFKLKDA KEDFTQFVRF ITGATTTGPG LDSPFVLLET PPESRPHTHA
     VLLRLSALHN NLVDLAKLES GGDAIELCID MWNPDAVSTV AKHVSVLRRI AKLPIIYSID
     AGALGLDARI SDPAVKNGDL YFQILEYGLR LGVEYLAIHL DHDHTRLTQI VQSRGMTKII
     GHFTIDISSG ISWEDEACLS IYIEAERLGC QLVRIVRLAT TREENDSVRK FVDRVKALSG
     SHPPIIAFNI GPIGRSSQVF NNTLTSVAHP AISPSALRAS DPQITSQDAI RALVQSYMLD
     PLKFYILGAS VAYSISPAMH NAAYASCGLS HVYRIPDAPS LALLDEWCHD PHFGGSSVSP
     CRAIGAINTV MPLRTSADGN IYPLSEQASR RNEAGPIAAW WGENTDWISI MVCLRRNLSP
     RNAISPIRTT GLVIGAGGMA RAAIYAMLQL GCRKIFILNR TLSRAEEVAR HFNSWVASSH
     TESDAAVRVL RSADEPWPSE LAFPSMIVSC VPENRIQGQP PANFVMPLQW LGSPSGGVVV
     ELAYNSLDTP LVRQLRRYRE ETDTPWVLID GLEIVAEQGF AQWELMTGRK APRRLMMTEV
     LRNYMGENGR LDEKTIRARL DAFSG
//
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