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Unplaced genomic scaffold GYMLUscaffold_14, whole genome shotgun sequence

 A0A0D0BIH8_9AGAR        Unreviewed;      1595 AA.
A0A0D0BIH8;
29-APR-2015, integrated into UniProtKB/TrEMBL.
29-APR-2015, sequence version 1.
12-SEP-2018, entry version 34.
RecName: Full=Pentafunctional AROM polypeptide {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 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-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};
Includes:
RecName: Full=Shikimate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03143};
EC=1.1.1.25 {ECO:0000256|HAMAP-Rule:MF_03143};
ORFNames=GYMLUDRAFT_241133 {ECO:0000313|EMBL:KIK63900.1};
Gymnopus luxurians FD-317 M1.
Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
Agaricomycetes; Agaricomycetidae; Agaricales; Omphalotaceae; Gymnopus.
NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK63900.1, ECO:0000313|Proteomes:UP000053593};
[1] {ECO:0000313|EMBL:KIK63900.1, ECO:0000313|Proteomes:UP000053593}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK63900.1,
ECO:0000313|Proteomes:UP000053593};
DOE Joint Genome Institute;
Mycorrhizal Genomics Consortium;
Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
Lipzen A., Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H.,
Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
"Evolutionary Origins and Diversification of the Mycorrhizal
Mutualists.";
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|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00712173}.
-!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
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|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858949}.
-!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00629607}.
-!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate =
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00712174}.
-!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate +
NADPH. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712180}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-
Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514};
-!- 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|PIRNR:PIRNR000514, 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|PIRNR:PIRNR000514, 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|PIRNR:PIRNR000514, 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|PIRNR:PIRNR000514, 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|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712169}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712187}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629599}.
-!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase
family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712186}.
-!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase
family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, 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|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712184}.
-!- SIMILARITY: In the C-terminal section; belongs to the shikimate
dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712181}.
-!- SIMILARITY: In the N-terminal section; belongs to the
dehydroquinate synthase family. {ECO:0000256|PIRNR:PIRNR000514}.
-!- 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}.
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EMBL; KN834762; KIK63900.1; -; Genomic_DNA.
EnsemblFungi; KIK63900; KIK63900; GYMLUDRAFT_241133.
UniPathway; UPA00053; UER00085.
UniPathway; UPA00053; UER00086.
UniPathway; UPA00053; UER00087.
UniPathway; UPA00053; UER00088.
UniPathway; UPA00053; UER00089.
Proteomes; UP000053593; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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_00210; EPSP_synth; 1.
HAMAP; MF_03143; Pentafunct_AroM; 1.
HAMAP; MF_00222; Shikimate_DH_AroE; 1.
HAMAP; MF_00109; Shikimate_kinase; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR016037; DHQ_synth_AroB.
InterPro; IPR030960; DHQS/DOIS.
InterPro; IPR001381; DHquinase_I.
InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
InterPro; IPR006264; EPSP_synthase.
InterPro; IPR023193; EPSP_synthase_CS.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; IPR010110; Shikimate_DH_AroM-type.
InterPro; IPR022893; Shikimate_DH_fam.
InterPro; IPR000623; Shikimate_kinase/TSH1.
InterPro; IPR023000; Shikimate_kinase_CS.
InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
Pfam; PF01761; DHQ_synthase; 1.
Pfam; PF01487; DHquinase_I; 1.
Pfam; PF00275; EPSP_synthase; 1.
Pfam; PF01488; Shikimate_DH; 1.
Pfam; PF08501; Shikimate_dh_N; 1.
Pfam; PF01202; SKI; 1.
PIRSF; PIRSF000514; Pentafunct_AroM; 1.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF55205; SSF55205; 1.
TIGRFAMs; TIGR01356; aroA; 1.
TIGRFAMs; TIGR01357; aroB; 1.
TIGRFAMs; TIGR01093; aroD; 1.
TIGRFAMs; TIGR01809; Shik-DH-AROM; 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|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858978};
Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858978};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00629580};
Complete proteome {ECO:0000313|Proteomes:UP000053593};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629621};
Kinase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629577};
Lyase {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00629772};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, 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|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712172};
Reference proteome {ECO:0000313|Proteomes:UP000053593};
Transferase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629577};
Zinc {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00712179}.
DOMAIN 83 368 DHQ_synthase. {ECO:0000259|Pfam:PF01761}.
DOMAIN 418 847 EPSP_synthase.
{ECO:0000259|Pfam:PF00275}.
DOMAIN 1310 1391 Shikimate_dh_N.
{ECO:0000259|Pfam:PF08501}.
DOMAIN 1426 1508 Shikimate_DH. {ECO:0000259|Pfam:PF01488}.
NP_BIND 47 49 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 88 91 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 119 121 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 144 145 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 881 888 ATP. {ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 1 393 3-dehydroquinate synthase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 199 202 Substrate binding 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 273 277 Substrate binding 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 1305 1595 Shikimate dehydrogenase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 269 269 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 284 284 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 835 835 For EPSP synthase activity.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 1194 1194 Proton acceptor; for 3-dehydroquinate
dehydratase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 1222 1222 Schiff-base intermediate with substrate;
for 3-dehydroquinate dehydratase
activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 199 199 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 280 280 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 296 296 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 124 124 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 135 135 Substrate 1. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 151 151 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 157 157 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 166 166 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 167 167 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 195 195 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 259 259 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 280 280 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 296 296 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 365 365 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
SEQUENCE 1595 AA; 172521 MW; 01865B366D3120FA CRC64;
MAATSTDVRR ISILGKDSIH CGFHLIPYIV HTVLTQLSAS TYVLITDSNI AKFHLTTFEN
EFDSALSSLS NGTHARPRFL SHIISPGELS KSREGKAAIE DFLLLNKCTR DTVILALGGG
VVGDLVGFVA ATFMRGVRFC QIPTSLLAMV DSSVGGKTAI DTPRGKNLIG AFWQPEFIFI
DAAMLETLPS REFSNGMAEV VKTAAIWDAA EFDSLESRSA EIFAAIQTPS VNHAGRSKKT
RSQAQELLLS VIVGSISVKS HIVTIDPTEK GLRNLVNFGH SIGHAIEAVL TPTILHGECV
SIGMVLEAEL SRQMGILSQV SVGRLTRCLK AYNLPVSLSD PRIANLPASK LITIERILDI
MKVDKKNRGT EKRIVLLSRI GATHEQQATP VPDALISKTL SESVTVVPGR PSFNPVKMTT
PGSKSISNRA LVLAALGTGT CRLKNLLHSD DTQVMMAALS ELKGAKFEWE DGGETLVVHG
GQGSLSVPPK GKELYLGNAG TAARFLTSVC TLVQKSPNDE ADTTVITGNA RMKQRPIGPL
VTALRANGSE IDYLESEGCL PLSIRPNGLK GGNIQLAASV SSQYVSSVLL CAPYANEPIT
LELIGGQVIS QPYIDMTIAM MKTFGIQVAR RAEEGTGKLL DIYDIPKGSY QNPAEYSIES
DASSATYPLA IAAITGTSCT IQNIGSASLQ GDARFAREVL ERMGCQVSQT ATETTVQGPP
MGQLKAVEEI DMEVMTDAFL TATALAAVAN GKTRIIGIAN QRVKECNRIR AMIDELAKFG
VSTIELDDGL EIIGKPIEEL KKGASVHCYD DHRVAMAFSV LASIITGTIL EEKRCVEKTW
PNWWDDLQNK IGLEVKGVEL ATPSVSVSST SDAHKSVVLI GMRGTGKTFI GDLAASALHW
TCIDADVHFE TVHSIGVRQF VQEHGWPAFR DAETNLLKDL LTQRGHNHVI SLGGGIVETS
AARDLLKDWV SKGGRVVHVV RNIDEVVEYL GVEGSRPAYG EPITEVFKRR APWFAECSSH
RFINHVEAFA DGKIVIDPTD TKRGVREEVA RFFDHITGIS ANLSPNLTSG RRSYFLSLTY
PDVMVALPKL EELSAGVDAL EVRVDLLRDH SEGYVADQIA ALRRVTSLPL IFTVRSVAEG
GAFPDNAHKE ALQLLNLALG LGVEYIDVEM RLPEQGIRQL VGRKGASQII ASWHEWTGRL
KWNSPEAQTM YEIASRTGDI VKMVFTASTM QDNFDCQTFA AKMNGRPNAK PFIAINMGAS
GQLSRVLNPT FSPVSHPLQP TRAAPGQISF AQVQKALHLI GELPAKKFYL FGSPIAHSLS
PTLHNSAFEL LGLPHTYSLL ETSDVGSEIE NTISEPDFGG ASVTIPHKLN IIPLLDQLTP
AAKAMGAVNT IVPMDSNSKR VLVGDNTDWL GIRGSIAARI AVGHIHSALV IGAGGTSRAA
IYALHSLGAK VIYLWNRTHS RAEELVTSFR PDIDVRIVDK LGEWSEDVVA PNVIVSTIPA
SETCLESSSE PEHLVYPASL FAYTSGPAIV LDLAYKPVET PLLKLAKLTA SNWDTAQGVE
VLLQQGYAQF EKWTGRRCPQ GPVSRNVWKV YNSRA


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XGC-Roche-16SMetaG12 Deep Sequencing of 16S amplicon Metagenome: Library preparation using V3-V4 region-400-500bp (customized region), data generation using long read shotgun approach on Roche GSFLX 12 samples
GE-102 Equine Skeletal Muscles Genomic DNA Species: Horse Tissue Genomic DNA 0.1mg


 

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