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Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); Shikimate dehydrogenase (EC 1.1.1.25); Shikimate kinase (SK) (EC 2.7.1.71)]

 A0A063BLV6_9HYPO        Unreviewed;      1459 AA.
A0A063BLV6;
03-SEP-2014, integrated into UniProtKB/TrEMBL.
03-SEP-2014, sequence version 1.
27-SEP-2017, entry version 30.
RecName: Full=Pentafunctional AROM polypeptide {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=Shikimate kinase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=SK {ECO:0000256|HAMAP-Rule:MF_03143};
EC=2.7.1.71 {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=3-dehydroquinate synthase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=DHQS {ECO:0000256|HAMAP-Rule:MF_03143};
EC=4.2.3.4 {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=3-dehydroquinate dehydratase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=3-dehydroquinase {ECO:0000256|HAMAP-Rule:MF_03143};
EC=4.2.1.10 {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=Shikimate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03143};
EC=1.1.1.25 {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000256|HAMAP-Rule:MF_03143};
EC=2.5.1.19 {ECO:0000256|HAMAP-Rule:MF_03143};
AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=EPSP synthase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=EPSPS {ECO:0000256|HAMAP-Rule:MF_03143};
ORFNames=UV8b_7539 {ECO:0000313|EMBL:KDB11616.1};
Ustilaginoidea virens.
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Hypocreales;
Hypocreales incertae sedis; Ustilaginoidea.
NCBI_TaxID=1159556 {ECO:0000313|EMBL:KDB11616.1, ECO:0000313|Proteomes:UP000027002};
[1] {ECO:0000313|EMBL:KDB11616.1, ECO:0000313|Proteomes:UP000027002}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=UV-8b {ECO:0000313|EMBL:KDB11616.1,
ECO:0000313|Proteomes:UP000027002};
Zhang Y., Zhang K., Fang A., Han Y., Yang J., Xue M., Bao J., Hu D.,
Zhou B., Sun X., Li S., Wen M., Yao N., Ma L.-J., Liu Y., Zhang M.,
Huang F., Luo C., Zhou L., Li J., Chen Z., Miao J., Wang S., Lai J.,
Xu J., Hsiang T., Peng Y.-L., Sun W.;
"Specific adaptation of Ustilaginoidea virens in occupying host
florets revealed by comparative and functional genomics.";
Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic
reactions in prechorismate polyaromatic amino acid biosynthesis.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712173}.
-!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712185}.
-!- CATALYTIC ACTIVITY: 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
= 3-dehydroquinate + phosphate. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00858949}.
-!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00629607}.
-!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate =
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712174}.
-!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate +
NADPH. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00712180}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|HAMAP-Rule:MF_03143};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-
Rule:MF_03143};
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 2/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00858971}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 3/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00712175}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 4/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00712177}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 5/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00629576}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 6/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00712169}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00712187}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00629599}.
-!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase
family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00712186}.
-!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase
family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00712182}.
-!- SIMILARITY: In the 4th section; belongs to the type-I 3-
dehydroquinase family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00712184}.
-!- SIMILARITY: In the C-terminal section; belongs to the shikimate
dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00712181}.
-!- SIMILARITY: In the N-terminal section; belongs to the sugar
phosphate cyclases superfamily. Dehydroquinate synthase family.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00858969}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03143}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KDB11616.1}.
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EMBL; JHTR01000064; KDB11616.1; -; Genomic_DNA.
EnsemblFungi; KDB11616; KDB11616; UV8b_7539.
UniPathway; UPA00053; UER00085.
UniPathway; UPA00053; UER00086.
UniPathway; UPA00053; UER00087.
UniPathway; UPA00053; UER00088.
UniPathway; UPA00053; UER00089.
Proteomes; UP000027002; Unassembled WGS sequence.
GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-UniRule.
GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; 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; cd00502; DHQase_I; 1.
CDD; cd01556; EPSP_synthase; 1.
CDD; cd00464; SK; 1.
Gene3D; 3.20.20.70; -; 1.
Gene3D; 3.65.10.10; -; 2.
HAMAP; MF_00110; DHQ_synthase; 1.
HAMAP; MF_00210; EPSP_synth; 1.
HAMAP; MF_03143; Pentafunct_AroM; 1.
HAMAP; MF_00109; Shikimate_kinase; 1.
InterPro; IPR018508; 3-dehydroquinate_DH_AS.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR016037; DHQ_synth_AroB.
InterPro; IPR030960; DHQS/DOIS.
InterPro; IPR001381; DHquinase_I.
InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
InterPro; IPR006264; EPSP_synthase.
InterPro; IPR023193; EPSP_synthase_CS.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008289; Pentafunct_AroM.
InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
InterPro; IPR031322; Shikimate/glucono_kinase.
InterPro; IPR013708; Shikimate_DH-bd_N.
InterPro; IPR000623; Shikimate_kinase/TSH1.
InterPro; IPR023000; Shikimate_kinase_CS.
Pfam; PF01761; DHQ_synthase; 1.
Pfam; PF01487; DHquinase_I; 1.
Pfam; PF00275; EPSP_synthase; 1.
Pfam; PF08501; Shikimate_dh_N; 1.
Pfam; PF01202; SKI; 1.
PIRSF; PIRSF000514; Pentafunct_AroM; 2.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF55205; SSF55205; 1.
TIGRFAMs; TIGR01356; aroA; 1.
TIGRFAMs; TIGR01357; aroB; 1.
TIGRFAMs; TIGR01093; aroD; 1.
PROSITE; PS01028; DEHYDROQUINASE_I; 1.
PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
PROSITE; PS01128; SHIKIMATE_KINASE; 1.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00858978};
Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00858978};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00629580};
Complete proteome {ECO:0000313|Proteomes:UP000027002};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00629621};
Kinase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00629577};
Lyase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00629772};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00727050};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00629584};
NADP {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712176};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00629580};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00712172};
Reference proteome {ECO:0000313|Proteomes:UP000027002};
Transferase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00629577};
Zinc {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712179}.
DOMAIN 54 332 DHQ_synthase. {ECO:0000259|Pfam:PF01761}.
DOMAIN 377 806 EPSP_synthase.
{ECO:0000259|Pfam:PF00275}.
DOMAIN 1264 1344 Shikimate_dh_N.
{ECO:0000259|Pfam:PF08501}.
NP_BIND 60 63 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 91 93 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 116 117 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 156 159 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 842 849 ATP. {ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 1 358 3-dehydroquinate synthase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 171 174 Substrate binding 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 238 242 Substrate binding 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 1259 1459 Shikimate dehydrogenase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 234 234 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 249 249 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 794 794 For EPSP synthase activity.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 1149 1149 Proton acceptor; for 3-dehydroquinate
dehydratase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 1177 1177 Schiff-base intermediate with substrate;
for 3-dehydroquinate dehydratase
activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 171 171 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 245 245 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 261 261 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 96 96 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 107 107 Substrate 1. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 123 123 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 129 129 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 138 138 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 139 139 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 167 167 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 224 224 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 245 245 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 261 261 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 330 330 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
SEQUENCE 1459 AA; 160627 MW; 6FF232C10CCAE5E2 CRC64;
MAESHRIPIQ KISVIGEDSI IAQYGLWPGF VAEDLLRHVK STTEDTTNAR LLTYAISPGE
ASKSRETKAE IEDWMLSQKC TRDIVIIALG GGVIGDMIGY VASTFMRGVR FVQVPTTLLA
MVDSSIGGKT AIDTPMGKNL IGAFWQPRRI YIDLAFIQTL PAREFINGMA EVIKTAAIWS
EDDFSILEKS ASEIMSCVRS KEEHRLVPIK EVLEKIIICS AKVKAEVVST DEREGGLRNL
LNFGHSIGHA IEAILTPQLL HGEAVAIGMI KEAELARYLG VLRPHALSRL SKCIAAYGLP
TSLSDGRVVK LTAGKKCQVD TILLKMAVDK KNDGDKKKIV LLSKIGGTFE QRASVVVDRD
IRTILSASIS VQPGVPDNLD VTVTPPGSKS ISNRALILAA LGSGSCRIKN LLHSDDTEYM
LSAIEQLGGA SYSWHNAGEI LEVEGRGGRL CASGDELYIG NAGTASRFLT TVLALCSPVK
GAQSTVLTGN ARMKVRPIGS LVDALRLNGV KIEYLEQEKS LPLRVHAGEG LQGGTIELAA
TVSSQYVSSI LMAAPYARTP VTLRLIGGKP ISQPYIDMTI SMMRTFGISV VRSSDEADTY
HIPQGVYKNP TEYVIESDAS SATYPLAVAA ITGTTCTVPN IGSASLQGDA RFAIDVLRPM
GCCVEQDQHR TTVTGPALGQ LRPLTHVDME PMTDAFLTAS VLAAVANGKT RITGIANQRV
KECNRISAMR EQLANFGICC VELDDGIEVI GRSLSDLQKP KAVIHCYDDH RVAMSFSVLS
TVAPGFTVIT EKDCVSKTWP GWWDTLALSF DVRLDGSDEA EVVTRSSSSK EECARRSIFV
IGMRGAGKTT AGRWIAKILD WKFVDLDEEL ERRLGMTIPD IISGPPGWDG FRREELRLLQ
EFMENVPEGH IFSCGGGIVE TPKARELLQA YCGAGGTVIS VRREIDQVIE YLSRDKTRPA
YTTEIRNVYE RRKPWYDLCS NHVYYSPHSA ADTKLDGRQT IPEDFKRFVF SITAGNHNLS
SVAAKNESFF ISLTAPNIKG NLSVVRNAVV GCDAVEIRID LLDNWALDSV TEQIAFIRYA
SKLPLIFTVR TVAQGGRFPD MAINERLDLC RLALKLGVEY LDVEVTSPDE MLQELSENRR
NTIIISSHHD LSGSLHWRNA SWVPIYNRAL QYGNVIKLVG HAETIEDNFE LLRFKNRMAT
ARENPVIAIN MGAAGKLSRL LNKFLTPVSH PALPFKAAPG QLSAVEIRQG RALLGEINKR
NFYLFGSPIL QSRSPALHNA LFKSLGLPHE YHLYDTNSVA ELQEMFQDEA FGGASVTIPL
KRDIIPLLDE LTPAAQIIGA VNTIIPQQQG KSTNKRYLPS HMMKYAEYPG RSRSSSVASP
PIVQSILWFK ILFLQYFLNP HSQMVTASSW KWRTNHIGHK LWNWLNRLVD GRRYLDLTYS
CHRVGISSKH GQVFNHCMS


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U0167b CLIA Bos taurus,Bovine,Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS 96T
U0167r CLIA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds,Rat,Rattus norvegicus 96T


 

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