Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q5B0P4

- Q5B0P4_EMENI

UniProt

Q5B0P4 - Q5B0P4_EMENI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

3-isopropylmalate dehydratase

Gene

AN5886.2

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.UniRule annotation

Catalytic activityi

(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate.UniRule annotation

Pathwayi

GO - Molecular functioni

  1. 3-isopropylmalate dehydratase activity Source: UniProtKB-EC
  2. 4 iron, 4 sulfur cluster binding Source: InterPro
  3. homoaconitate hydratase activity Source: ASPGD
  4. isomerase activity Source: UniProtKB-KW

GO - Biological processi

  1. cellular response to farnesol Source: ASPGD
  2. leucine biosynthetic process Source: ASPGD
  3. lysine biosynthetic process via aminoadipic acid Source: ASPGD
Complete GO annotation...

Keywords - Molecular functioni

IsomeraseImported, LyaseUniRule annotation

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Leucine biosynthesisUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00048; UER00071.

Names & Taxonomyi

Protein namesi
Recommended name:
3-isopropylmalate dehydrataseUniRule annotation (EC:4.2.1.33UniRule annotation)
Alternative name(s):
Alpha-IPM isomeraseUniRule annotation
Isopropylmalate isomeraseUniRule annotation
Gene namesi
ORF Names:AN5886.2Imported, ANIA_05886Imported
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)Imported
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560: Chromosome I

Subcellular locationi

GO - Cellular componenti

  1. 3-isopropylmalate dehydratase complex Source: InterPro
Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00007148.

Family & Domainsi

Sequence similaritiesi

Belongs to the aconitase/IPM isomerase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0065.
HOGENOMiHOG000226972.
KOiK01702.
OMAiCVIEFAG.
OrthoDBiEOG7W41M9.

Family and domain databases

Gene3Di3.20.19.10. 1 hit.
3.30.499.10. 3 hits.
3.40.1060.10. 1 hit.
HAMAPiMF_01026. LeuC_type1.
MF_01031. LeuD_type1.
InterProiIPR004430. 3-IsopropMal_deHydase_lsu.
IPR004431. 3-IsopropMal_deHydase_ssu.
IPR012235. 3-IsopropMal_deHydtase_ssu/lsu.
IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR015937. Acoase/IPM_deHydtase.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 1 hit.
PfamiPF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF001418. ACN. 1 hit.
PRINTSiPR00415. ACONITASE.
SUPFAMiSSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
TIGRFAMsiTIGR00170. leuC. 1 hit.
TIGR00171. leuD. 1 hit.
PROSITEiPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5B0P4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPGADRKPKT LYDKVFDHHI VNEQEDGTVL IYIDRHLVHE VTSPQAFEGL
60 70 80 90 100
KNANRKVRRP DCTLVTVDHN IPTSSRKNFK NVEQFIEEND SRLQCSTLEE
110 120 130 140 150
NVKDFGLTYF GMDDKRQGIV HVIGPEQGFT LPGTTVVCGD SHTSTHGAFG
160 170 180 190 200
ALAFGIGTSE VEHVLATQTL ITRRSKNMRV QVDGELPAGV TSKDVVLHII
210 220 230 240 250
GLIGTAGGTG CVIEFCGSVI RGLSMEARMS MCNMSIEGGA RAGMVAPDET
260 270 280 290 300
TFEYLKGRPL APKYDSAEWK KAVSYWSSLA SDEDAVYDKT ILIDAKDIVP
310 320 330 340 350
TISWGTSPQD VVPITGVVPG PDDFEDEARK AACKRALEYM GLTAGTPMKD
360 370 380 390 400
VTVDKVFIGS CTNSRIEDLR AAANVVRGKK VASNIKRAMV VPGSGLVKQQ
410 420 430 440 450
AEAEGLDKIF IDAGFEWREA GCSMCLGMNP DILSPQERCA STSNRNFEGR
460 470 480 490 500
QGAGGRTHLM SPAMAAAAAI VGKLADVREH IAESPRLGKV QPKVDVKPEA
510 520 530 540 550
EDVDTEEELD HILDQPADNE PHTNTHTPAT TSAGLPKFTT LKGIAAPMDR
560 570 580 590 600
SNVDTDAIIP KQFLKTIKRT GLGSALFYEL RYKDGQEDPS FILNQGIYRN
610 620 630 640 650
SKILVVTGPN FGCGSSREHA PWALLDFGIK CVIAPSFADI FFNNTFKNGM
660 670 680 690 700
LPVVIPDQAV LEKIADEARA GREVEVDLVN QEIKDEAGNK LASFDVDAFR
710 720 730 740 750
KHCLINGLDD IGLTLQMEDK IAKFEAKRTL DTPWLDGKAY LKRGRTGGSN
760 770
MVKAAPVPKT NRGDVKGEPL EW
Length:772
Mass (Da):84,105
Last modified:April 26, 2005 - v1
Checksum:i06E769007FB6BD14
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BN001301 Genomic DNA. Translation: CBF70635.1.
AACD01000100 Genomic DNA. Translation: EAA58395.1.
RefSeqiXP_663490.1. XM_658398.1.

Genome annotation databases

EnsemblFungiiCADANIAT00007148; CADANIAP00007148; CADANIAG00007148.
GeneIDi2870766.
KEGGiani:AN5886.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BN001301 Genomic DNA. Translation: CBF70635.1 .
AACD01000100 Genomic DNA. Translation: EAA58395.1 .
RefSeqi XP_663490.1. XM_658398.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 162425.CADANIAP00007148.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANIAT00007148 ; CADANIAP00007148 ; CADANIAG00007148 .
GeneIDi 2870766.
KEGGi ani:AN5886.2.

Phylogenomic databases

eggNOGi COG0065.
HOGENOMi HOG000226972.
KOi K01702.
OMAi CVIEFAG.
OrthoDBi EOG7W41M9.

Enzyme and pathway databases

UniPathwayi UPA00048 ; UER00071 .

Family and domain databases

Gene3Di 3.20.19.10. 1 hit.
3.30.499.10. 3 hits.
3.40.1060.10. 1 hit.
HAMAPi MF_01026. LeuC_type1.
MF_01031. LeuD_type1.
InterProi IPR004430. 3-IsopropMal_deHydase_lsu.
IPR004431. 3-IsopropMal_deHydase_ssu.
IPR012235. 3-IsopropMal_deHydtase_ssu/lsu.
IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR015937. Acoase/IPM_deHydtase.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view ]
PANTHERi PTHR11670. PTHR11670. 1 hit.
Pfami PF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF001418. ACN. 1 hit.
PRINTSi PR00415. ACONITASE.
SUPFAMi SSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
TIGRFAMsi TIGR00170. leuC. 1 hit.
TIGR00171. leuD. 1 hit.
PROSITEi PS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., Ait-zahra M., Allen N., Allen T., An P., Anderson M., Anderson S., Arachchi H., Armbruster J., Bachantsang P., Baldwin J., Barry A., Bayul T., Blitshsteyn B.
    , Bloom T., Blye J., Boguslavskiy L., Borowsky M., Boukhgalter B., Brunache A., Butler J., Calixte N., Calvo S., Camarata J., Campo K., Chang J., Cheshatsang Y., Citroen M., Collymore A., Considine T., Cook A., Cooke P., Corum B., Cuomo C., David R., Dawoe T., Degray S., Dodge S., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A., Elkins T., Engels R., Erickson J., Farina A., Faro S., Ferreira P., Fischer H., Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G., Gnerre S., Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Hatcher B., Heller A., Higgins H., Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E., Iliev I., Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M., Karlsson E., Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E., Labutti K., Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T., Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., Lui A., Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., Manning J., Marabella R., Maru K., Matthews C., Mauceli E., Mccarthy M., Mcdonough S., Mcghee T., Meldrim J., Meneus L., Mesirov J., Mihalev A., Mihova T., Mikkelsen T., Mlenga V., Moru K., Mozes J., Mulrain L., Munson G., Naylor J., Newes C., Nguyen C., Nguyen N., Nguyen T., Nicol R., Nielsen C., Nizzari M., Norbu C., Norbu N., O'donnell P., Okoawo O., O'leary S., Omotosho B., O'neill K., Osman S., Parker S., Perrin D., Phunkhang P., Piqani B., Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V., Raymond C., Retta R., Richardson S., Rise C., Rodriguez J., Rogers J., Rogov P., Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T., Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C., Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., Stetson K., Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., Tenzing P., Tesfaye S., Theodore J., Thoulutsang Y., Topham K., Towey S., Tsamla T., Tsomo N., Vallee D., Vassiliev H., Venkataraman V., Vinson J., Vo A., Wade C., Wang S., Wangchuk T., Wangdi T., Whittaker C., Wilkinson J., Wu Y., Wyman D., Yadav S., Yang S., Yang X., Yeager S., Yee E., Young G., Zainoun J., Zembeck L., Zimmer A., Zody M., Lander E.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: FGSC A4.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4Imported and FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139Imported.
  3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139Imported.
  4. "The 2008 update of the Aspergillus nidulans genome annotation: A community effort."
    Russo Wortman J., Mabey Gilsenan J., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J.M., Durek P., Espeso E., Fekete E., Flipphi M., Garcia Estrada C.
    , Geysens S., Goldman G., de Groot P.W.J., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A.K.W., Kim J-M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., MacCabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Posci I., Punt P.J., Ram A.F.J., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van der Vondervoot P.J.I., de Vries R.P., Walton J., Xiang X., Xiong Y., Ping Zeng A., Brandt B.W., Cornell M.J., van den Hondel C.A.M.J.J., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-S13(2009)
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: FGSC A4Imported.

Entry informationi

Entry nameiQ5B0P4_EMENI
AccessioniPrimary (citable) accession number: Q5B0P4
Secondary accession number(s): C8UZW6
Entry historyi
Integrated into UniProtKB/TrEMBL: April 26, 2005
Last sequence update: April 26, 2005
Last modified: October 29, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3