ID A0A0M8P6E3_9EURO Unreviewed; 905 AA.
AC A0A0M8P6E3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KOS46098.1};
GN ORFNames=ACN38_g2948 {ECO:0000313|EMBL:KOS46098.1};
OS Penicillium nordicum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS46098.1, ECO:0000313|Proteomes:UP000037696};
RN [1] {ECO:0000313|EMBL:KOS46098.1, ECO:0000313|Proteomes:UP000037696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS46098.1,
RC ECO:0000313|Proteomes:UP000037696};
RA Nguyen H.D., Seifert K.A.;
RT "Genome sequencing of Penicillium nordicum.";
RL Submitted (AUG-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:KOS46098.1}.
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DR EMBL; LHQQ01000033; KOS46098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8P6E3; -.
DR STRING; 229535.A0A0M8P6E3; -.
DR OrthoDB; 2256238at2759; -.
DR Proteomes; UP000037696; 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:SF27; 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 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000037696}.
FT DOMAIN 566..646
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 708..752
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 848..878
FT /note="SDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18317"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 905 AA; 99915 MW; 8476DE07BA8428B2 CRC64;
MSMLVRPPKR KLHEVEASDN GPRKYSSGVG LSPTVQLSSR PSSSQLSEYR EAFGDSRLPS
LKELQSNRGS PVLFENGHLQ TPRTFSPKAS VVLIGIRGTG KSSLAVILAA TSGRRLIDAD
RYFQQSVGYS RAVFKKENDG SVYRQQEARV FESMLADNQE GCVIACGAGS MERNGQRLLR
EFAQTHPVIH VIRDPESIQS YLKAWDTQKV RHFLELSGPI YRGCSNLEFF NLSEARSEDL
SNDSGDNSPP THRTEPRPHT PIPFLTLKRV QRDFLRFIAF ITGDIVELNS QHASFPLSLL
PVESRMYTSA VSVPFSKVCE RGVDIEQLEF TADAFELAVD VTGSPGQPGL SSSLADSISQ
AVALIRRNII VPLIYHVESY TTSTGSLSPS QVPVRSTDEA YLNLVRHGLR LSTGFLTVDL
TRDDNIISQI IFASGRTRII GHFEAFHPLP GGWDGDEYMK VYERAKSLGC DIVRVCQPAE
TPEDNLAVQR FRHRIQSLPV AGLSLVAYNT GPLGRISRCF NPILSPVTHP SLVTEVPTHL
RSYITAREVQ NALYSSFALD PMQFFVFGAN TTYSMSPAMH NTAFKVCGLP HNYSIHQSPT
LRGLNDLVEN QYFGGSSVSL PYKTECIPLL HSMSAHARAI GAVNTLIPIR NLDDLDDTRL
QESSIFLQKS RAGPIKGLHG DNTDWIGICN CIRRGLSPAN AVRLSSTGLV IGSGGMARAA
IYSMIHLGVQ NIFVYNRTLA NAERLAHHYN RQDLHSKEAG GSGRPTVRII ASLSDPWPVD
FKQPTIVVSG IPAHSIGGEP APNFRLPAQW LESPTGGVVV DLAYKPLNTP LMKQTRALSH
RGWVALDGLD VLPEQGFAQF ELFTGRRAPR RVMRSIVLQE YKDDEGNNDH EAIQDRLQQM
DGQPT
//
