ID I3IQI0_9BACT Unreviewed; 492 AA.
AC I3IQI0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00214, ECO:0000256|HAMAP-Rule:MF_00222};
DE Includes:
DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000256|HAMAP-Rule:MF_00214};
DE Short=3-dehydroquinase {ECO:0000256|HAMAP-Rule:MF_00214};
DE EC=4.2.1.10 {ECO:0000256|HAMAP-Rule:MF_00214};
DE AltName: Full=Type I DHQase {ECO:0000256|HAMAP-Rule:MF_00214};
DE AltName: Full=Type I dehydroquinase {ECO:0000256|HAMAP-Rule:MF_00214};
DE Short=DHQ1 {ECO:0000256|HAMAP-Rule:MF_00214};
DE Includes:
DE RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000256|HAMAP-Rule:MF_00222};
DE Short=SDH {ECO:0000256|HAMAP-Rule:MF_00222};
DE EC=1.1.1.25 {ECO:0000256|HAMAP-Rule:MF_00222};
GN Name=aroE {ECO:0000256|HAMAP-Rule:MF_00222};
GN Synonyms=aroD {ECO:0000256|HAMAP-Rule:MF_00214};
GN ORFNames=KSU1_D0666 {ECO:0000313|EMBL:GAB63975.1};
OS Candidatus Jettenia caeni.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Brocadiaceae; Candidatus Jettenia.
OX NCBI_TaxID=247490 {ECO:0000313|EMBL:GAB63975.1, ECO:0000313|Proteomes:UP000002985};
RN [1] {ECO:0000313|EMBL:GAB63975.1, ECO:0000313|Proteomes:UP000002985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22673575; DOI=10.1016/j.febslet.2012.04.041;
RA Hira D., Toh H., Migita C.T., Okubo H., Nishiyama T., Hattori M.,
RA Furukawa K., Fujii T.;
RT "Anammox organism KSU-1 expresses a NirK-type copper-containing nitrite
RT reductase instead of a NirS-type with cytochrome cd1.";
RL FEBS Lett. 586:1658-1663(2012).
CC -!- FUNCTION: Involved in the biosynthesis of the chorismate, which leads
CC to the biosynthesis of aromatic amino acids. Catalyzes the reversible
CC NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate
CC (SA). {ECO:0000256|HAMAP-Rule:MF_00222}.
CC -!- FUNCTION: Involved in the third step of the chorismate pathway, which
CC leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-
CC dehydration of 3-dehydroquinate (DHQ) and introduces the first double
CC bond of the aromatic ring to yield 3-dehydroshikimate.
CC {ECO:0000256|HAMAP-Rule:MF_00214}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
CC Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00214};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH;
CC Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25;
CC Evidence={ECO:0000256|ARBA:ARBA00001648, ECO:0000256|HAMAP-
CC Rule:MF_00222};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 3/7. {ECO:0000256|HAMAP-Rule:MF_00214}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 4/7. {ECO:0000256|ARBA:ARBA00004871, ECO:0000256|HAMAP-Rule:MF_00222}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00214}.
CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC {ECO:0000256|HAMAP-Rule:MF_00222}.
CC -!- SIMILARITY: Belongs to the type-I 3-dehydroquinase family.
CC {ECO:0000256|HAMAP-Rule:MF_00214}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00214}.
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:GAB63975.1}.
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DR EMBL; BAFH01000004; GAB63975.1; -; Genomic_DNA.
DR AlphaFoldDB; I3IQI0; -.
DR STRING; 247490.KSU1_D0666; -.
DR eggNOG; COG0169; Bacteria.
DR eggNOG; COG0710; Bacteria.
DR OrthoDB; 9792692at2; -.
DR UniPathway; UPA00053; UER00086.
DR Proteomes; UP000002985; Unassembled WGS sequence.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019632; P:shikimate metabolic process; 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 HAMAP; MF_00214; AroD; 1.
DR HAMAP; MF_00222; Shikimate_DH_AroE; 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; IPR041121; SDH_C.
DR InterPro; IPR011342; Shikimate_DH.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR022893; Shikimate_DH_fam.
DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR NCBIfam; TIGR01093; aroD; 1.
DR NCBIfam; TIGR00507; aroE; 1.
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 SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00214};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_00214}; Lyase {ECO:0000256|HAMAP-Rule:MF_00214};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00222};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00222};
KW Reference proteome {ECO:0000313|Proteomes:UP000002985};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_00214}.
FT DOMAIN 221..301
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 334..406
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 455..483
FT /note="SDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18317"
FT ACT_SITE 109
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00214"
FT ACT_SITE 134
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00214"
FT ACT_SITE 278
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 29..31
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00214"
FT BINDING 56
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00214"
FT BINDING 172
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00214"
FT BINDING 193
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00214"
FT BINDING 197
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00214"
FT BINDING 229..231
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 274
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 299
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 314
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 347..351
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 432
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 434
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 455
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 462
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
SQ SEQUENCE 492 AA; 54822 MW; E9291E2C71D5162D CRC64;
MICVPIIADN LEDALKDIAE ASEVADIVEL RIDYIKDLNL KRLLKGCIKP VIVTNRPVRE
GGKFTGSEED RISLLKLAVE LQVDYIDVEH DSIQKVNNTG KTKRIVSYHN FDKTPDDLTG
IFQRLKQSGA DIIKIVPYAN GITDNVKIYQ LLQQVDMPTI SFCMGEYGII SRILYKKFGS
YLTFASLQSG KESAPGQVSI HELLNTYHVR RQDKHTSIYG LIGNPVSHSI SPAIHNTLFK
EMGFHNIYVP FKVDTIGNFI REFRGLDIKG YSVTIPHKES VMGHLDGIDQ IAKKIGAVNT
IVNRDGRLIG FNTDCEAAVR VLEDINNVSG MAAKAGSLQG KKVTLFGAGG VARAIAFGLK
EREAQITIFN RNYERAQSLA CEVDCFYRKF SDLPALEADI VVNATSVGMF PSVHETPIDK
NYLKPNMIVF DTVYNPPETR LLRDAKSLGC RTVGGLSMFV HQAAAQYKLW TGQMPSLELI
EKIAYKKLYH GE
//
