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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)]

 A0A0C2YNM3_BIFAD        Unreviewed;       539 AA.
A0A0C2YNM3;
01-APR-2015, integrated into UniProtKB/TrEMBL.
01-APR-2015, sequence version 1.
20-JUN-2018, entry version 34.
RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00109, ECO:0000256|HAMAP-Rule:MF_00110};
Includes:
RecName: Full=Shikimate kinase {ECO:0000256|HAMAP-Rule:MF_00109};
Short=SK {ECO:0000256|HAMAP-Rule:MF_00109};
EC=2.7.1.71 {ECO:0000256|HAMAP-Rule:MF_00109};
Includes:
RecName: Full=3-dehydroquinate synthase {ECO:0000256|HAMAP-Rule:MF_00110};
Short=DHQS {ECO:0000256|HAMAP-Rule:MF_00110};
EC=4.2.3.4 {ECO:0000256|HAMAP-Rule:MF_00110};
Name=aroB {ECO:0000256|HAMAP-Rule:MF_00110};
Synonyms=aroK {ECO:0000256|HAMAP-Rule:MF_00109};
ORFNames=AAX71_03885 {ECO:0000313|EMBL:KLE27845.1},
BBK15_05385 {ECO:0000313|EMBL:OFA34903.1},
LU08_06345 {ECO:0000313|EMBL:KIM01360.1};
Bifidobacterium adolescentis.
Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
Bifidobacterium.
NCBI_TaxID=1680 {ECO:0000313|EMBL:KIM01360.1, ECO:0000313|Proteomes:UP000031974};
[1] {ECO:0000313|EMBL:KIM01360.1, ECO:0000313|Proteomes:UP000031974}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IVS-1 {ECO:0000313|EMBL:KIM01360.1,
ECO:0000313|Proteomes:UP000031974};
Frese S.A., Hutkins R.W., Walter J.;
Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:KIM01360.1, ECO:0000313|Proteomes:UP000031974}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IVS-1 {ECO:0000313|EMBL:KIM01360.1,
ECO:0000313|Proteomes:UP000031974};
Krumbeck J.A., Maldonado-Gomez M.X., Martinez I., Burkey T.E.,
Ramer-Tait A., Harris E.N.;
"Introducing the concept of In Vivo Selection to identify probiotic
stains for synergistic synbiotic applications.";
Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|EMBL:KLE27845.1, ECO:0000313|Proteomes:UP000035571}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=150 {ECO:0000313|EMBL:KLE27845.1,
ECO:0000313|Proteomes:UP000035571};
Dyachkova M.S., Klimina K.M., Kovtun A.S., Zakharevich N.V.,
Nezametdinova V.Z., Averina O.V., Danilenko V.N.;
"Draft genome sequences of Bifidobacterium angulatum strain 102 and
Bifidobacterium adolescentis strain 150: focusing on the genes
responsible for communication with the host organism.";
Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|EMBL:OFA34903.1, ECO:0000313|Proteomes:UP000175684}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Km 4 {ECO:0000313|EMBL:OFA34903.1,
ECO:0000313|Proteomes:UP000175684};
Danilenko V.N.;
"Draft Genome Sequence of Bifidobacterium adolescentis strain Km 4.";
Submitted (JUL-2016) 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_00110}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KIM01360.1}.
-----------------------------------------------------------------------
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EMBL; JRNZ01000030; KIM01360.1; -; Genomic_DNA.
EMBL; LBHQ01000003; KLE27845.1; -; Genomic_DNA.
EMBL; MAXD01000003; OFA34903.1; -; Genomic_DNA.
RefSeq; WP_033499428.1; NZ_NAQF01000002.1.
EnsemblBacteria; KIM01360; KIM01360; LU08_06345.
EnsemblBacteria; KLE27845; KLE27845; AAX71_03885.
EnsemblBacteria; OFA34903; OFA34903; BBK15_05385.
PATRIC; fig|1680.6.peg.1395; -.
eggNOG; ENOG4105D49; Bacteria.
eggNOG; COG0337; LUCA.
eggNOG; COG0703; LUCA.
UniPathway; UPA00053; UER00085.
UniPathway; UPA00053; UER00088.
Proteomes; UP000031974; Unassembled WGS sequence.
Proteomes; UP000035571; Unassembled WGS sequence.
Proteomes; UP000175684; 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:UP000031974,
ECO:0000313|Proteomes:UP000035571, ECO:0000313|Proteomes:UP000175684};
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};
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 238 503 DHQ_synthase. {ECO:0000259|Pfam:PF01761}.
NP_BIND 13 18 ATP. {ECO:0000256|HAMAP-Rule:MF_00109}.
NP_BIND 242 247 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}.
NP_BIND 276 280 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}.
NP_BIND 300 301 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}.
METAL 17 17 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00109}.
METAL 355 355 Cobalt or zinc. {ECO:0000256|HAMAP-
Rule:MF_00110}.
METAL 427 427 Cobalt or zinc; via tele nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00110}.
METAL 443 443 Cobalt or zinc; via tele nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00110}.
BINDING 35 35 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00109}.
BINDING 59 59 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00109}.
BINDING 81 81 Substrate; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00109}.
BINDING 123 123 ATP. {ECO:0000256|HAMAP-Rule:MF_00109}.
BINDING 141 141 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00109}.
BINDING 158 158 ATP. {ECO:0000256|HAMAP-Rule:MF_00109}.
BINDING 313 313 NAD; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_00110}.
BINDING 322 322 NAD. {ECO:0000256|HAMAP-Rule:MF_00110}.
SEQUENCE 539 AA; 59113 MW; D8C90912FD9F4B4E CRC64;
MRRPVAVIIG MMGAGKTRVG KEAAQMMQLP FADADNEIEH DAGMKIPEYF ERYGEPEFRK
LESDVVLDML EDFDGIFSLG GGAPMTPSIQ QGLAEYIADG GKVVYLMADP KEAMERANRG
GGRPMLNGDA NERWKKLYKE RDPVFRRVAN VQVRTHGQTP QVAARKLMEM IDQRIVHVTG
STIEPYDVCI GEGVMSQLAQ VLGDKPAKVA LIHTQAVQRH SDRARTLLRQ SGYDVHDIVI
PDAEAGKTIE VANGIWQRLG EEGFTRSDAI VGLGGGAATD LAGFVAATWM RGIRYVNCPT
SLLAMVDAST GGKTGINTPQ GKNLVGSFYT PAGVLADMGA LASLPNDIFI EGLGEVAKSG
FIMDPEILRM LEDHADELRS FDGSTFLDSD LKDVVAELIE RTVTVKAYHV SADLKEAGLR
EFLNYGHTLG HAIEKLEHFR WRHGNAVAVG CVYAAELSHL LGYIDQDLVD YHRSLLGSLG
LPTSWNNGSW DDVLALMHRD KKARGNKLRF VILGSLGHPI HLEDPPADAV EEAFRRIQR


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