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Unplaced genomic scaffold supercont1.2, whole genome shotgun sequence

 A0A0D2F669_XYLBA        Unreviewed;      1602 AA.
A0A0D2F669;
29-APR-2015, integrated into UniProtKB/TrEMBL.
29-APR-2015, sequence version 1.
05-DEC-2018, entry version 37.
RecName: Full=Pentafunctional AROM polypeptide {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=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-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};
ORFNames=Z519_01280 {ECO:0000313|EMBL:KIW97696.1};
Cladophialophora bantiana CBS 173.52.
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
Cladophialophora.
NCBI_TaxID=1442370 {ECO:0000313|EMBL:KIW97696.1, ECO:0000313|Proteomes:UP000053789};
[1] {ECO:0000313|EMBL:KIW97696.1, ECO:0000313|Proteomes:UP000053789}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CBS 173.52 {ECO:0000313|EMBL:KIW97696.1,
ECO:0000313|Proteomes:UP000053789};
The Broad Institute Genomics Platform;
Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J.,
Nusbaum C., Birren B.;
"The Genome Sequence of Cladophialophora bantiana CBS 173.52.";
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:
Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000256|HAMAP-
Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00712185};
-!- CATALYTIC ACTIVITY:
Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-
carboxyvinyl)-3-phosphoshikimate + phosphate;
Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701,
ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19;
Evidence={ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712174};
-!- CATALYTIC ACTIVITY:
Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-
dehydroquinate + phosphate; Xref=Rhea:RHEA:21968,
ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394;
EC=4.2.3.4; Evidence={ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858949};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+);
Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216;
EC=2.7.1.71; Evidence={ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00287328};
-!- CATALYTIC ACTIVITY:
Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH;
Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630,
ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
EC=1.1.1.25; Evidence={ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514};
-!- 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 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:SAAS00336886}.
-!- 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; KN846981; KIW97696.1; -; Genomic_DNA.
RefSeq; XP_016624365.1; XM_016759037.1.
EnsemblFungi; KIW97696; KIW97696; Z519_01280.
GeneID; 27694208; -.
UniPathway; UPA00053; UER00089.
Proteomes; UP000053789; 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.
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; 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:SAAS00415286};
Complete proteome {ECO:0000313|Proteomes:UP000053789};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00415327};
Kinase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00415285};
Lyase {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00415747};
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:SAAS00415250};
NADP {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712176};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00415286};
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:SAAS00415285};
Zinc {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00712179}.
DOMAIN 82 364 DHQ_synthase. {ECO:0000259|Pfam:PF01761}.
DOMAIN 409 841 EPSP_synthase.
{ECO:0000259|Pfam:PF00275}.
DOMAIN 1306 1386 Shikimate_dh_N.
{ECO:0000259|Pfam:PF08501}.
NP_BIND 50 52 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 87 90 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 120 122 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 145 146 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 185 188 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 877 884 ATP. {ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 1 390 3-dehydroquinate synthase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 200 203 Substrate binding 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 270 274 Substrate binding 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 870 1062 Shikimate kinase. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 1301 1602 Shikimate dehydrogenase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 266 266 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 281 281 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 829 829 For EPSP synthase activity.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 1189 1189 Proton acceptor; for 3-dehydroquinate
dehydratase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 1218 1218 Schiff-base intermediate with substrate;
for 3-dehydroquinate dehydratase
activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 200 200 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 277 277 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 293 293 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 125 125 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 136 136 Substrate 1. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 152 152 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 158 158 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 167 167 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 168 168 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 196 196 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 256 256 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 277 277 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 293 293 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 362 362 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
SEQUENCE 1602 AA; 174256 MW; 59AA37DD9ABFEBD8 CRC64;
MPLVNGTAKE VRVSLLGKES IIINFGLWRN YVASDLLSNL ESSTYVLITD TNLGSLYTKS
FQEAFENASQ QKEKSARLLM HQIPPGESSK SRQTKDDIED WLLSQSPPCG RDTVIIALGG
GVVGDLTGFV AATYMRGVRF VQVPTTLLAM VDSSIGGKTA IDTPLGKNLV GAIWQPQRIY
IDLDFLGTLP RRELINGMAE VIKTAAISDE EEFIELERHA ERIMAAVNAD ISQGASRFKD
VEATLIRIIS ASAKFKAHVV TIDERETGLR NLLNFGHSIG HAIEAFLTPQ VLHGECVAIG
MIKEAELARY LGILSGVAVG RLQKCLTTYG LPTRLDDERV RKLSGGKVCT VDGMLKKMGV
DKKNDGAKKK VVLLSGIGRT YEQKASVVSD SDLRVVLSPS VEVVPGVPKD LNVVCTPPGS
KSISNRALVL AALGHGTCRI KNLLTSADTE VMLEALTRLG AATFSWEEDG EVLVVNGNGG
RLEATQHELY LGNAGTAARF LTSVATLTRQ SHVASTVLTG NARMKQRPIG DLVDALRENG
AGIEYMENNG SLPLNVTASA GFNGGEIKLA AKVSSQYVSS LLMCAPYAKK PVTLRLVGGK
PVSQPYIDMT IAMMVSFGVP VQKSKTEEHT YHIPQGIYLN PTEYVVESDA SSATYPLAIA
AITGTTCTIP NIGSASLQGD SAFATDVLRP MGCQVKQTLT STTVTGPRDG KLVPLANIDM
EPMTDAFLTA SVLAAVAQGG KSNTTRIYGI ANQRVKECNR IQAMEDELAK FGVTCRQFDD
GIEVDGIDRT RLRRPQGGVY CYDDHRVAMS FSVLALAAPQ STLILEKECT GKTWPGWWDT
MALRFNVKLE GVELQEIAEH AKAKKLDRSA ASIFIIGMRG AGKTTSGRWA ARSLGKKLVD
LDTELETREG MSIPEIIKGQ GWGYFRKREL ELLKSVMKDM PNGYVFACGG GVVETQEARN
LLVAWHEKNG HVLLVERDIN EVMDFLQIDK TRPAYVEDMM GVWLRRKPWF EQCSNLLYYS
QSIPNEQMSE AAEDFDRFLQ MVTGKIDVLS KFKRKSETFF ASLTFPDLRP HLKILPEVCL
GSDAVELRVD LLKDPNSDST IPSTDYVTSQ LSLLRATVPL PVVFTIRTKS QGGKFPDEAY
AEYLHLCTLA IRMGSEFLDL EVASFPESVL SPILSFKNRS NTRIIASHHD PQGTLSWSKP
GSWISIYNKC LQYGDIVKLI GVAGILDDNF ALRRFKQWSN SQHPDLPLIA INMGRTGQIS
RVLNGFMTPV SHPSLPFKAA PGQLSACEIR HGLTLIGEIV PKKFYLFGSP ISASKSPELH
NTLFKETGLP HVYSLCETTD LAVIKEIIRA EDFGGASVTI PLKLDVMPLL DDVDASARLI
GAVNTIVPVS NPISGKNSLV GYNTDFLGMM DCLRTAGASA ALGEGEQSGL VIGGGGTARA
AIHTLHKMGY KPIYLIGRNQ GKMEELARTF PPLYDLVLLD AERSGATEQK MTTPPVVAIA
TIPADMPIDP PLAASLQKIF SRSALLATST APKGQGTSAP TRTLLELAYK PAHTAVMQMA
EEVGGWKTVQ GLETLVTQGL WQFEYWTGIR VRGLGGRISR VS


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