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Q5B0P4 (Q5B0P4_EMENI) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3-isopropylmalate dehydratase PIRNR PIRNR001418
EC=4.2.1.33 PIRNR PIRNR001418
Alternative name(s):
Alpha-IPM isomerase PIRNR PIRNR001418
Isopropylmalate isomerase PIRNR PIRNR001418
Gene names
ORF Names:AN5886.2 EMBL EAA58395.1, ANIA_05886 EMBL CBF70635.1
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome] EMBL EAA58395.1
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella ›

Protein attributes

Sequence length772 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate By similarity. PIRNR PIRNR001418

Catalytic activity

(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. PIRNR PIRNR001418

Pathway

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. PIRNR PIRNR001418

Sequence similarities

Belongs to the aconitase/IPM isomerase family. PIRNR PIRNR001418

Sequences

Sequence LengthMass (Da)Tools
Q5B0P4 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 06E769007FB6BD14

FASTA77284,105
        10         20         30         40         50         60 
MPGADRKPKT LYDKVFDHHI VNEQEDGTVL IYIDRHLVHE VTSPQAFEGL KNANRKVRRP 

        70         80         90        100        110        120 
DCTLVTVDHN IPTSSRKNFK NVEQFIEEND SRLQCSTLEE NVKDFGLTYF GMDDKRQGIV 

       130        140        150        160        170        180 
HVIGPEQGFT LPGTTVVCGD SHTSTHGAFG ALAFGIGTSE VEHVLATQTL ITRRSKNMRV 

       190        200        210        220        230        240 
QVDGELPAGV TSKDVVLHII GLIGTAGGTG CVIEFCGSVI RGLSMEARMS MCNMSIEGGA 

       250        260        270        280        290        300 
RAGMVAPDET TFEYLKGRPL APKYDSAEWK KAVSYWSSLA SDEDAVYDKT ILIDAKDIVP 

       310        320        330        340        350        360 
TISWGTSPQD VVPITGVVPG PDDFEDEARK AACKRALEYM GLTAGTPMKD VTVDKVFIGS 

       370        380        390        400        410        420 
CTNSRIEDLR AAANVVRGKK VASNIKRAMV VPGSGLVKQQ AEAEGLDKIF IDAGFEWREA 

       430        440        450        460        470        480 
GCSMCLGMNP DILSPQERCA STSNRNFEGR QGAGGRTHLM SPAMAAAAAI VGKLADVREH 

       490        500        510        520        530        540 
IAESPRLGKV QPKVDVKPEA EDVDTEEELD HILDQPADNE PHTNTHTPAT TSAGLPKFTT 

       550        560        570        580        590        600 
LKGIAAPMDR SNVDTDAIIP KQFLKTIKRT GLGSALFYEL RYKDGQEDPS FILNQGIYRN 

       610        620        630        640        650        660 
SKILVVTGPN FGCGSSREHA PWALLDFGIK CVIAPSFADI FFNNTFKNGM LPVVIPDQAV 

       670        680        690        700        710        720 
LEKIADEARA GREVEVDLVN QEIKDEAGNK LASFDVDAFR KHCLINGLDD IGLTLQMEDK 

       730        740        750        760        770 
IAKFEAKRTL DTPWLDGKAY LKRGRTGGSN MVKAAPVPKT NRGDVKGEPL EW

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"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. expand/collapse author list , 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 / M139.
[3]"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. expand/collapse author list , 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 A4 EMBL CBF70635.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BN001301 Genomic DNA. Translation: CBF70635.1.
AACD01000100 Genomic DNA. Translation: EAA58395.1.
RefSeqXP_663490.1. XM_658398.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00007148.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00007148; CADANIAP00007148; CADANIAG00007148.
GeneID2870766.
KEGGani:AN5886.2.

Phylogenomic databases

eggNOGCOG0065.
HOGENOMHOG000226972.
KOK01702.
OMASMEARMS.
OrthoDBEOG40S3PS.

Enzyme and pathway databases

UniPathwayUPA00048; UER00071.

Family and domain databases

Gene3D3.20.19.10. 1 hit.
3.30.499.10. 3 hits.
3.40.1060.10. 1 hit.
HAMAPMF_01026. LeuC_type1.
MF_01031. LeuD_type1.
InterProIPR004430. 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]
PANTHERPTHR11670. PTHR11670. 1 hit.
PfamPF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PIRSFPIRSF001418. ACN. 1 hit.
PRINTSPR00415. ACONITASE.
SUPFAMSSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit.
SSF53732. Aconitase_N. 1 hit.
TIGRFAMsTIGR00170. leuC. 1 hit.
TIGR00171. leuD. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ5B0P4_EMENI
AccessionPrimary (citable) accession number: Q5B0P4
Secondary accession number(s): C8UZW6
Entry history
Integrated into UniProtKB/TrEMBL: April 26, 2005
Last sequence update: April 26, 2005
Last modified: April 3, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info