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Multifunctional fusion protein [Includes: Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4)]

 T2I0L4_BIFLN            Unreviewed;       540 AA.
T2I0L4;
13-NOV-2013, integrated into UniProtKB/TrEMBL.
13-NOV-2013, sequence version 1.
23-MAY-2018, entry version 35.
SubName: Full=3-dehydroquinate synthase {ECO:0000313|EMBL:CCK34864.1};
EC=4.2.3.4 {ECO:0000313|EMBL:CCK34864.1};
Name=aroB {ECO:0000256|HAMAP-Rule:MF_00110,
ECO:0000313|EMBL:CCK34864.1};
Synonyms=aroK {ECO:0000256|HAMAP-Rule:MF_00109};
ORFNames=BN57_1035 {ECO:0000313|EMBL:CCK34864.1};
Bifidobacterium longum subsp. longum CECT 7347.
Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
Bifidobacterium.
NCBI_TaxID=1205679 {ECO:0000313|EMBL:CCK34864.1, ECO:0000313|Proteomes:UP000018160};
[1] {ECO:0000313|EMBL:CCK34864.1, ECO:0000313|Proteomes:UP000018160}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CECT 7347 {ECO:0000313|EMBL:CCK34864.1,
ECO:0000313|Proteomes:UP000018160};
Chenoll E., Codoner F., Sanz Y., Genoves S., Ramon D.;
"Safety assessment of strain Bifidobacterium longum CECT 7347, a
probiotic able to reduce the toxicity and inflammatory potential of
gliadin-derived peptides, based on phenotypic traits, whole genome
sequencing and murine trials.";
Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-
heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
{ECO:0000256|HAMAP-Rule:MF_00110}.
-!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl
group of shikimic acid using ATP as a cosubstrate.
{ECO:0000256|HAMAP-Rule:MF_00109}.
-!- CATALYTIC ACTIVITY: 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
= 3-dehydroquinate + phosphate. {ECO:0000256|HAMAP-Rule:MF_00110}.
-!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate.
{ECO:0000256|HAMAP-Rule:MF_00109}.
-!- COFACTOR:
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000256|HAMAP-Rule:MF_00110};
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|HAMAP-Rule:MF_00110};
Note=Binds 1 divalent metal cation per subunit. Can use either
Co(2+) or Zn(2+). {ECO:0000256|HAMAP-Rule:MF_00110};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00109};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_00109};
-!- COFACTOR:
Name=NAD(+); Xref=ChEBI:CHEBI:57540;
Evidence={ECO:0000256|HAMAP-Rule:MF_00110,
ECO:0000256|SAAS:SAAS00961751};
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 2/7. {ECO:0000256|HAMAP-Rule:MF_00110}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 5/7. {ECO:0000256|HAMAP-Rule:MF_00109}.
-!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00109}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00109}.
-!- SIMILARITY: Belongs to the shikimate kinase family.
{ECO:0000256|HAMAP-Rule:MF_00109}.
-!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily.
Dehydroquinate synthase family. {ECO:0000256|HAMAP-Rule:MF_00110}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00109}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:CCK34864.1}.
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EMBL; CALH01000058; CCK34864.1; -; Genomic_DNA.
RefSeq; WP_022527566.1; NZ_CALH01000058.1.
EnsemblBacteria; CCK34864; CCK34864; BN57_1035.
UniPathway; UPA00053; UER00085.
UniPathway; UPA00053; UER00088.
Proteomes; UP000018160; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0004765; F:shikimate kinase 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.
CDD; cd00464; SK; 1.
HAMAP; MF_00110; DHQ_synthase; 1.
HAMAP; MF_00109; Shikimate_kinase; 1.
InterPro; IPR016037; DHQ_synth_AroB.
InterPro; IPR030960; DHQS/DOIS.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR031322; Shikimate/glucono_kinase.
InterPro; IPR000623; Shikimate_kinase/TSH1.
Pfam; PF01761; DHQ_synthase; 1.
Pfam; PF01202; SKI; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR01357; aroB; 1.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00109};
Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00109};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00109};
Cobalt {ECO:0000256|HAMAP-Rule:MF_00110};
Complete proteome {ECO:0000313|Proteomes:UP000018160};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00109};
Kinase {ECO:0000256|HAMAP-Rule:MF_00109};
Lyase {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00958949,
ECO:0000313|EMBL:CCK34864.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00109};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00109};
NAD {ECO:0000256|HAMAP-Rule:MF_00110, ECO:0000256|SAAS:SAAS00961758};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00109};
Transferase {ECO:0000256|HAMAP-Rule:MF_00109};
Zinc {ECO:0000256|HAMAP-Rule:MF_00110}.
DOMAIN 239 504 DHQ_synthase. {ECO:0000259|Pfam:PF01761}.
NP_BIND 14 19 ATP. {ECO:0000256|HAMAP-Rule:MF_00109}.
NP_BIND 243 248 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}.
NP_BIND 277 281 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}.
NP_BIND 301 302 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}.
NP_BIND 341 344 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}.
METAL 18 18 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00109}.
METAL 356 356 Cobalt or zinc. {ECO:0000256|HAMAP-
Rule:MF_00110}.
METAL 428 428 Cobalt or zinc; via tele nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00110}.
METAL 444 444 Cobalt or zinc; via tele nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00110}.
BINDING 36 36 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00109}.
BINDING 60 60 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00109}.
BINDING 82 82 Substrate; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00109}.
BINDING 124 124 ATP. {ECO:0000256|HAMAP-Rule:MF_00109}.
BINDING 142 142 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00109}.
BINDING 314 314 NAD; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_00110}.
BINDING 323 323 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}.
SEQUENCE 540 AA; 58694 MW; 47A9CB23F97D5B5B CRC64;
MTARPRAVII GMMGAGKTRV GKEVAHMLRL PFADADVEIE REVGMKIPSY FEEYGEPAFR
EVEADLIADM LEDFDGIFSL GGGAPMTPST QHALASYIDH GGRVVYLDAD PAEAMERANR
GGGRPMLNGN ANSRWKKLFK QRDPVFREVA NVHVHTRGLT PQGAAKKVID MVSERAVHVT
GAAIEPYDVV IGEGAMNHLV DVLGPKPAKI ALIHTQPVQR HSDRARALLR QGGYEVSDIV
IPDAEPGKTI TVANGIWERL GNEGFTRSDA VVGLGGGAAT DLAGFVAATW MRGVRYVNCP
TSLLAMVDAS TGGKTGINTP QGKNLVGSFY TPAGVLADTK TLATLPNDIF IEGLGEVAKS
GFIRDPEILH ILEDHAAELR AFDGSTFLGS PLEDVVAELI ERTVKVKAYH VSSDLKEKGL
REFLNYGHTM GHAIEKLEHF RWRHGNAVAV GMVYAAELAH LIGYIDQDLV DYHRSLLASL
GLPTSWNGGS FDDVLALMHR DKKARGNELR FVVLDEIGHV VHLDNPPAEA VEEAFRRIQQ


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