ID A0A430FT66_9BIFI Unreviewed; 310 AA.
AC A0A430FT66;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=shikimate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00012962};
DE EC=1.1.1.25 {ECO:0000256|ARBA:ARBA00012962};
GN ORFNames=D2E26_0580 {ECO:0000313|EMBL:RSX56017.1};
OS Bifidobacterium dolichotidis.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=2306976 {ECO:0000313|EMBL:RSX56017.1, ECO:0000313|Proteomes:UP000287609};
RN [1] {ECO:0000313|EMBL:RSX56017.1, ECO:0000313|Proteomes:UP000287609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2036B {ECO:0000313|EMBL:RSX56017.1,
RC ECO:0000313|Proteomes:UP000287609};
RA Lugli G.A., Duranti S., Milani C.;
RT "Characterization of the phylogenetic diversity of five novel species
RT belonging to the genus Bifidobacterium.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 4/7. {ECO:0000256|ARBA:ARBA00004871}.
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:RSX56017.1}.
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DR EMBL; QXGM01000001; RSX56017.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A430FT66; -.
DR OrthoDB; 9776868at2; -.
DR UniPathway; UPA00053; UER00087.
DR Proteomes; UP000287609; Unassembled WGS sequence.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
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 InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR022893; Shikimate_DH_fam.
DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR PANTHER; PTHR21089:SF1; BIFUNCTIONAL 3-DEHYDROQUINATE DEHYDRATASE_SHIKIMATE DEHYDROGENASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR21089; SHIKIMATE DEHYDROGENASE; 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000287609}.
FT DOMAIN 8..89
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 129..247
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
SQ SEQUENCE 310 AA; 33552 MW; 4651516521DD1840 CRC64;
MVLHRCAVLG QPIAHSLSPV LHNAAYMALG VEDWEYTRAE VGEQDLPAFL AGLDDTWVGL
SLTMPLKRTI IPYGKLRNRW ARQLKVANTA VMHYDETVRS IDLYNTDVYG IACAFQHALY
EQGTVPKRNS TMLILGNGNT AASAVAAAVM MGCVDQVIVA ARHVEKTETL RELVAVQSNT
MKPLQSIALS DAAQAMAQAD LIVNTIPGLG ADVVAQQFME LNLSAKPDAL LLDVVYAPRV
TQLMNAFSQA DGTSISGIEM LIYQAIAQVL LMTGVDPSFN ADDVQSGQPN VLGMLENAMR
TALEEALQHE
//
