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Unplaced genomic scaffold supercont1.218, whole genome shotgun sequence

 A0A0D0Y2G2_9TREE        Unreviewed;      1610 AA.
A0A0D0Y2G2;
29-APR-2015, integrated into UniProtKB/TrEMBL.
29-APR-2015, sequence version 1.
28-MAR-2018, entry version 31.
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=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=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-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=I306_06030 {ECO:0000313|EMBL:KIR76989.1};
Cryptococcus gattii EJB2.
Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
Tremellomycetes; Tremellales; Cryptococcaceae; Cryptococcus;
Cryptococcus gattii species complex.
NCBI_TaxID=1296103 {ECO:0000313|EMBL:KIR76989.1, ECO:0000313|Proteomes:UP000054272};
[1] {ECO:0000313|EMBL:KIR76989.1, ECO:0000313|Proteomes:UP000054272}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=EJB2 {ECO:0000313|EMBL:KIR76989.1,
ECO:0000313|Proteomes:UP000054272};
The Broad Institute Genomics Platform;
Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
Dromer F., Young S., Zeng Q., Gargeya S., Abouelleil A., Alvarado L.,
Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S.,
Hansen M., Howarth C., Imamovic A., Larimer J., Murphy C., Naylor J.,
Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
Wortman J., Nusbaum C., Birren B.;
"The Genome Sequence of Cryptococcus gattii EJB2.";
Submitted (JAN-2015) 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; KN848766; KIR76989.1; -; Genomic_DNA.
EnsemblFungi; KIR76989; KIR76989; I306_06030.
UniPathway; UPA00053; UER00085.
UniPathway; UPA00053; UER00086.
UniPathway; UPA00053; UER00087.
UniPathway; UPA00053; UER00088.
UniPathway; UPA00053; UER00089.
Proteomes; UP000054272; 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_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; 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; 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:UP000054272};
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};
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 78 365 DHQ_synthase. {ECO:0000259|Pfam:PF01761}.
DOMAIN 417 857 EPSP_synthase.
{ECO:0000259|Pfam:PF00275}.
DOMAIN 1336 1417 Shikimate_dh_N.
{ECO:0000259|Pfam:PF08501}.
DOMAIN 1453 1525 Shikimate_DH. {ECO:0000259|Pfam:PF01488}.
NP_BIND 47 49 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 84 87 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 115 117 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 140 141 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 180 183 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 899 906 ATP. {ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 1 391 3-dehydroquinate synthase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 195 198 Substrate binding 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 271 275 Substrate binding 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 1331 1610 Shikimate dehydrogenase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 267 267 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 282 282 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 845 845 For EPSP synthase activity.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 1220 1220 Proton acceptor; for 3-dehydroquinate
dehydratase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 1248 1248 Schiff-base intermediate with substrate;
for 3-dehydroquinate dehydratase
activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 195 195 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 278 278 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 294 294 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 120 120 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 131 131 Substrate 1. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 147 147 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 153 153 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 162 162 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 163 163 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 191 191 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 257 257 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 278 278 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 294 294 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 363 363 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
SEQUENCE 1610 AA; 173194 MW; 82AB15C434C2104B CRC64;
MSSSSADVLK ISILGSESIH VGFHLLPYIF ETVVTTLPSS TYVLITDTNL SAIYLNDLKA
SFEEATAQAG NKARFLVYEV APGEGAKSRK VKGEIEDWML DNKCTRDTVI LAFGGGVIGD
LAGFVAATFM RGVKFIQIPT TLLAMVDSSV GGKTAIDTPH GKNLIGAFWQ PSYIFVDLAF
LTTLPTREVS NGMAEVVKTA AIWKDDDFAL LESRSAEISL AASTRPTGSP TAGRFASDRS
HAQSLLLTVV SGSIYVKAHI VTIDERETGL RNLVNFGHTI GHAIEAILTP AMLHGECVSV
GIILEAEVAR QLGVLSQVAV GRLTRCLQAY GLPVSLSDRR ITALPASSQL SVDRLLDIMK
IDKKNSGPAK KIVLLSRIGK TYEEKASVVA DDVIRKVLCE SVTVKAAIPT KSPITMATPG
SKSISNRALV LAALGKGTCR VRNLLHSDDT AVMMNALVEL KGAVFSWEDG GDTIVVEGGG
GILSTPAKGK ELYLGNAGTA SRFLTTVCAM VSGSASSERS TIITGNARMK QRPIGPLVDA
LTANGAKVKY LESTGCLPLD IETDGFRGGH IQLAASVSSQ YVSSILLCAP YAAEQVTLEL
TGGQVISQPY IDMTIAMMEQ FGATVERQKD EQGNLLDIYV IPKCTYVNPA EYSVESDASS
ATYPLAIAAI TGTTCTISNI GSSSLQGDAR FAKEVLEPMG CTVEQTLTST KVTGPPVGTL
RALGNVDMEP MTDAFLTASV LAAVAVKPCL PERRVEGLPE TASRIYGIAN QRVKECNRIQ
AMRDQLAKFS VETDEFDDGI IIFGKPEASL FRGASIHCYD DHRVAMAFAV LSCIIDKTII
EEKRCVEKTW PNFWDDLQNK IGVTVEGVEL ETHNQASTSA KPTAAIDPSQ SDRPIFLIGM
RGAGKTYVGR MAADILSGQF TDADDVFAQE THQSVSEFVA VNGWDEFRKK ETEILSKFVE
EHRGNHVIAL GGGIVETETA RGILTAHVAK GGHVVHVTRA LEDIEAYLDS IGSTAVRPNW
GETFADVFKR REPWYQACSS HEFYNVLEAV GGQSQEEHTK AMRAECGRFF KFITGRESNR
PRLSTENPTS FLSLTFPDIT PALVHLDELT EGADAVEFRV DLLSITGQAP TGPALPPISF
VAKQLASLRL ATTLPIVFSV RSKDQGGMVP SDNAEAYGAL VRLGLRSACE YVDLEVCWPV
QVLDNIVRLK RETHIIASWH DWTGDMAWDG EEMKAKHLLC EKYGDVAKIV GTAKSGLDNA
KLALLVGEVR SRPGAKPLLA INMGAAGQLS RVLNPILTPV THDALPSRAA PGQLTAREII
QARALIGFLP AKKFVLFGCP IAHSVSPLLH NTGFATLGLP HNYELHESEK VDQDVLEVIR
SPDFGGASVT IPLKLDIIPH LDSVSEDAKI IGAVNTVIPR GGKLHGENTD WQAIRQAAAQ
NLDAGALSDG SFTALVIGAG GTCRAAIYAM HKLQFKTIYL FNRTSENAAK VKASFPESYN
IIVVTSLPLP EAPAVVVSTV PGNSLTLDTS SEGIYFPSDV LSRPSGVAID LAYKPHMTAL
LQAAEKKEGW KVVPGVEILC LQGFMQFEEW TGKRAPEKKM RKAVLDKYFA


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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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