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Shikimate dehydrogenase (NADP( )) (SDH) (EC 1.1.1.25)

 Q1PJ89_PROMR            Unreviewed;       301 AA.
Q1PJ89;
16-MAY-2006, integrated into UniProtKB/TrEMBL.
16-MAY-2006, sequence version 1.
25-OCT-2017, entry version 75.
RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000256|HAMAP-Rule:MF_00222, ECO:0000256|SAAS:SAAS00228653};
Short=SDH {ECO:0000256|HAMAP-Rule:MF_00222};
EC=1.1.1.25 {ECO:0000256|HAMAP-Rule:MF_00222, ECO:0000256|SAAS:SAAS00216361};
Name=aroE {ECO:0000256|HAMAP-Rule:MF_00222,
ECO:0000313|EMBL:ABE11495.1};
ORFNames=HOT0M-8F9_0010 {ECO:0000313|EMBL:ABE11495.1};
uncultured Prochlorococcus marinus clone HOT0M-8F9.
Bacteria; Cyanobacteria; Synechococcales; Prochloraceae;
Prochlorococcus.
NCBI_TaxID=379395 {ECO:0000313|EMBL:ABE11495.1};
[1] {ECO:0000313|EMBL:ABE11495.1}
NUCLEOTIDE SEQUENCE.
PubMed=16556843; DOI=10.1126/science.1122050;
Coleman M.L., Sullivan M.B., Martiny A.C., Steglich C., Barry K.,
Delong E.F., Chisholm S.W.;
"Genomic islands and the ecology and evolution of Prochlorococcus.";
Science 311:1768-1770(2006).
[2] {ECO:0000313|EMBL:ABE11495.1}
NUCLEOTIDE SEQUENCE.
US DOE Joint Genome Institute (JGI);
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
Hammon N., Israni S., Richardson P.;
"Sequencing of the draft fosmids and assembly of Prochlorococcus
marinus environmental genome fragment.";
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Involved in the biosynthesis of the chorismate, which
leads to the biosynthesis of aromatic amino acids. Catalyzes the
reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to
yield shikimate (SA). {ECO:0000256|HAMAP-Rule:MF_00222,
ECO:0000256|SAAS:SAAS00642229}.
-!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate +
NADPH. {ECO:0000256|HAMAP-Rule:MF_00222,
ECO:0000256|SAAS:SAAS00048714}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 4/7. {ECO:0000256|HAMAP-Rule:MF_00222,
ECO:0000256|SAAS:SAAS00179153}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00222,
ECO:0000256|SAAS:SAAS00179298}.
-!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
{ECO:0000256|HAMAP-Rule:MF_00222, ECO:0000256|SAAS:SAAS00634670}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00222}.
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EMBL; DQ366743; ABE11495.1; -; Genomic_DNA.
ProteinModelPortal; Q1PJ89; -.
UniPathway; UPA00053; UER00087.
GO; GO:0050661; F:NADP binding; IEA:InterPro.
GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0019632; P:shikimate metabolic process; IEA:InterPro.
HAMAP; MF_00222; Shikimate_DH_AroE; 1.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR011342; Shikimate_DH.
InterPro; IPR013708; Shikimate_DH-bd_N.
InterPro; IPR022893; Shikimate_DH_fam.
InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
Pfam; PF01488; Shikimate_DH; 1.
Pfam; PF08501; Shikimate_dh_N; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR00507; aroE; 1.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00222,
ECO:0000256|SAAS:SAAS00179155};
Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00222,
ECO:0000256|SAAS:SAAS00179155};
NADP {ECO:0000256|HAMAP-Rule:MF_00222, ECO:0000256|SAAS:SAAS00058194};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00222,
ECO:0000256|SAAS:SAAS00808825}.
DOMAIN 26 108 Shikimate_dh_N.
{ECO:0000259|Pfam:PF08501}.
DOMAIN 134 218 Shikimate_DH. {ECO:0000259|Pfam:PF01488}.
NP_BIND 144 148 NADP. {ECO:0000256|HAMAP-Rule:MF_00222}.
REGION 34 36 Shikimate binding. {ECO:0000256|HAMAP-
Rule:MF_00222}.
ACT_SITE 85 85 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00222}.
BINDING 81 81 Shikimate. {ECO:0000256|HAMAP-
Rule:MF_00222}.
BINDING 106 106 Shikimate. {ECO:0000256|HAMAP-
Rule:MF_00222}.
BINDING 122 122 Shikimate. {ECO:0000256|HAMAP-
Rule:MF_00222}.
BINDING 244 244 NADP; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_00222}.
BINDING 246 246 Shikimate. {ECO:0000256|HAMAP-
Rule:MF_00222}.
BINDING 267 267 NADP; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_00222}.
BINDING 274 274 Shikimate. {ECO:0000256|HAMAP-
Rule:MF_00222}.
SEQUENCE 301 AA; 33321 MW; 9A7C080E05666C31 CRC64;
MVPEQTITFR VKILNMISSK TSFIALIGNP VSHSLSPIMQ NAALQYLGLD LIYIAVPCKD
EDLELVLNSF KKINCKGLNI TIPHKEKVFN LCSEISPIAN KLKAINTLKL NSEKKWSATN
TDVEGFIYPL KNLNLAKKQS IVLGSGGAAR SVIQGLINLN LSTISVISRN KSSLDQLIKN
FENQIQLQGL LNSDDQAQIL IREADLIVNT TPAGMKTIQY ENNVLPYGEA FWTSLNSQTI
VYDLIYNPAP TSLLKFSAKK GCMTIDGLEM LVAQGIKSLS FWTDGLEVPF HVMNDALKKY
L


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