Q4X144 (Q4X144_ASPFU) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended 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:

AFUA_2G11260 EMBL EAL93421.1

Organism

Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome] EMBL EAL93421.1

Taxonomic identifier

330879 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Neosartorya fumigata

Protein attributes

Sequence length	777 AA.
Sequence status	Complete.
Protein existence	Inferred 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
Caution	The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. EMBL EAL93421.1

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Leucine biosynthesis PIRNR PIRNR001418
Molecular function	Lyase PIRNR PIRNR001418 EMBL EAL93421.1
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	leucine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	3-isopropylmalate dehydratase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	3-isopropylmalate dehydratase activity Inferred from electronic annotation. Source: EC 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q4X144 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: 0747087B4433D2B1	FASTA	777	84,077
	10 20 30 40 50 60 MPGVDKKPKT LYDKVLDHHI VNEQEDGTIL IYIDRHLVHE VTSPQAFEGL KNAGRKVRRP 70 80 90 100 110 120 DCTLATVDHN IPTSSRKNFK NVEEFIEETD SRLQCTTLEQ NVKDFGLTYF GMGDKRQGIV 130 140 150 160 170 180 HIIGPEQGFT LPGTTVVCGD SHTSTHGAFG ALAFGIGTSE VEHVLATQTL LTRRSKNMRI 190 200 210 220 230 240 QVDGELPPGV TSKDVVLHII GVIGTAGGTG AVIEFCGSVI RGLSMEARMS MCNMSIEAGA 250 260 270 280 290 300 RAGMIAPDET TFEYLKGRPL APKYDSAEWK RAVAFWSSLA SDEGAVYDKT VVLDGKDIIP 310 320 330 340 350 360 TVSWGTSPQD VVPITGVVPG PDDFEDENRK VACKRALEYM GLVAGTRIQD IPVDKVFIGS 370 380 390 400 410 420 CTNARIEDLR AAAKVVRGKK VAANIKRAMV VPGSGLVKQQ AEAEGLDRVF TDAGFEWREA 430 440 450 460 470 480 GCSMCLGMNP DILSPQERCA STSNRNFEGR QGAGGRTHLM SPAMAAAAAI TGHLADVREH 490 500 510 520 530 540 LTASPLLAKA QPHLDIQEEH EDPTTEDEFD RIMDMPADNE PHANSSAATA AAGSTAGLPK 550 560 570 580 590 600 FTTLRGIAAP MDRSNVDTDA IIPKQFLKTI KRTGLGSALF YELRYNPADG SENKSFVLNQ 610 620 630 640 650 660 EPYRNAKILV VTGPNFGCGS SREHAPWALL DFGIKCIIAP SFADIFFNNT FKNGMLPVVI 670 680 690 700 710 720 SDPAVLATIA AEASAGREIE VDLVNQEIKD AAGSKLASFE VDAFRKHCLI NGLDDIGLTL 730 740 750 760 770 QMEDKIRAFE AKRTLETPWL DGSGYLKRGN RGGATMIQAA PVPKTNRGDV KTEPLEW

References

[1]

"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W. Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAHF01000001 Genomic DNA. Translation: EAL93421.1.
RefSeq	XP_755459.1. XM_750366.1.
3D structure databases
ProteinModelPortal	Q4X144.
ModBase	Search...
Protein-protein interaction databases
STRING	5085.CADAFUAP00004794. Q4X144.
Protein family/group databases
Allergome	9531. Asp f IPMI.
Proteomic databases
PRIDE	Q4X144.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAFUAT00004794; CADAFUAP00004794; CADAFUAG00004794.
GeneID	3512897.
KEGG	afm:AFUA_2G11260.
Phylogenomic databases
HOGENOM	HOG000226972.
KO	K01702.
OMA	SMEARMS.
OrthoDB	EOG40S3PS.
Enzyme and pathway databases
UniPathway	UPA00048; UER00071.
Family and domain databases
Gene3D	3.20.19.10. 1 hit. 3.30.499.10. 3 hits. 3.40.1060.10. 1 hit.
HAMAP	MF_01026. LeuC_type1. MF_01031. LeuD_type1.
InterPro	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]
PANTHER	PTHR11670. PTHR11670. 1 hit.
Pfam	PF00330. Aconitase. 1 hit. PF00694. Aconitase_C. 1 hit. [Graphical view]
PIRSF	PIRSF001418. ACN. 1 hit.
PRINTS	PR00415. ACONITASE.
SUPFAM	SSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit. SSF53732. Aconitase_N. 1 hit.
TIGRFAMs	TIGR00170. leuC. 1 hit. TIGR00171. leuD. 1 hit.
PROSITE	PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q4X144_ASPFU

Accession

Primary (citable) accession number: Q4X144

Entry history

Integrated into UniProtKB/TrEMBL:	July 5, 2005
Last sequence update:	July 5, 2005
Last modified:	April 3, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)