ID F4BUZ8_METSG Unreviewed; 284 AA.
AC F4BUZ8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00012962, ECO:0000256|HAMAP-Rule:MF_00222};
DE Short=SDH {ECO:0000256|HAMAP-Rule:MF_00222};
DE EC=1.1.1.25 {ECO:0000256|ARBA:ARBA00012962, ECO:0000256|HAMAP-Rule:MF_00222};
GN Name=aroE {ECO:0000256|HAMAP-Rule:MF_00222,
GN ECO:0000313|EMBL:AEB69568.1};
GN OrderedLocusNames=MCON_3308 {ECO:0000313|EMBL:AEB69568.1};
OS Methanothrix soehngenii (strain ATCC 5969 / DSM 3671 / JCM 10134 / NBRC
OS 103675 / OCM 69 / GP-6) (Methanosaeta concilii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=990316 {ECO:0000313|EMBL:AEB69568.1, ECO:0000313|Proteomes:UP000007807};
RN [1] {ECO:0000313|EMBL:AEB69568.1, ECO:0000313|Proteomes:UP000007807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 5969 / DSM 3671 / JCM 10134 / NBRC 103675 / OCM 69 / GP-6
RC {ECO:0000313|Proteomes:UP000007807};
RX PubMed=21571998; DOI=10.1128/JB.05031-11;
RA Barber R.D., Zhang L., Harnack M., Olson M.V., Kaul R., Ingram-Smith C.,
RA Smith K.S.;
RT "Complete genome sequence of Methanosaeta concilii, a specialist in
RT aceticlastic methanogenesis.";
RL J. Bacteriol. 193:3668-3669(2011).
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 -!- 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|HAMAP-Rule:MF_00222};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 4/7. {ECO:0000256|HAMAP-Rule:MF_00222}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00222}.
CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC {ECO:0000256|HAMAP-Rule:MF_00222}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00222}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002565; AEB69568.1; -; Genomic_DNA.
DR RefSeq; WP_013720583.1; NC_015416.1.
DR AlphaFoldDB; F4BUZ8; -.
DR STRING; 990316.MCON_3308; -.
DR GeneID; 10462530; -.
DR KEGG; mcj:MCON_3308; -.
DR HOGENOM; CLU_044063_0_1_2; -.
DR InParanoid; F4BUZ8; -.
DR OrthoDB; 8744at2157; -.
DR UniPathway; UPA00053; UER00087.
DR Proteomes; UP000007807; Chromosome.
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; cd01065; NAD_bind_Shikimate_DH; 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_00222; Shikimate_DH_AroE; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
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; TIGR00507; aroE; 1.
DR PANTHER; PTHR21089:SF1; BIFUNCTIONAL 3-DEHYDROQUINATE DEHYDRATASE_SHIKIMATE DEHYDROGENASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR21089; SHIKIMATE DEHYDROGENASE; 1.
DR Pfam; PF18317; SDH_C; 1.
DR Pfam; PF01488; Shikimate_DH; 1.
DR Pfam; PF08501; Shikimate_dh_N; 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_00222};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_00222};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00222};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00222,
KW ECO:0000313|EMBL:AEB69568.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007807}.
FT DOMAIN 6..89
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 124..195
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 245..272
FT /note="SDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18317"
FT ACT_SITE 65
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 14..16
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 61
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 78
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 87
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 110
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 134..138
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 220
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 222
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 242
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 249
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
SQ SEQUENCE 284 AA; 30693 MW; 8494F3CCA7AE1A32 CRC64;
MKIFGIFGDP IEHSLSPAMQ NAAFRALGMD GCYHAFRVSR SRLKDAVIGA DAMGFGGLNL
TIPLKEEALS LDFLEADDLA RAIGAVNTIS FSGEAGEEKG KNRIQGYNTD GWGALSALQD
AGVKVKGSRV LLIGAGGAAR AIAYALDREG AEVSIANRNL KRAHELAASV GGISYCLCDL
EPLVRQADVI INATSVGMRE GDGRIIDSRL LKSHHVVFDI VYNRETELLW DARSIGAAAI
DGVMMLVYQG ARAFEIWTGR KAPADVMERA VRESLEERRQ RKSR
//
