Q42669 (ACOC_CUCMC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aconitate hydratase
Short name=Aconitase
EC=4.2.1.3

Alternative name(s):
Citrate hydro-lyase

Gene names

Name:

ACO

Organism

Cucumis melo var. conomon (Oriental pickling melon)

Taxonomic identifier

3657 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Cucurbitales › Cucurbitaceae › Benincaseae › Cucumis › Cucumis melo › Cucumis melo subsp. melo

Protein attributes

Sequence length	764 AA.
Sequence status	Fragment.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the isomerization of citrate to isocitrate via cis-aconitate By similarity.
Catalytic activity	Citrate = isocitrate.
Cofactor	Binds 1 4Fe-4S cluster per subunit By similarity.
Pathway	Carbohydrate metabolism; glyoxylate and dicarboxylate metabolism.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the aconitase/IPM isomerase family.

Ontologies

Keywords
Biological process	Glyoxylate bypass
Cellular component	Cytoplasm
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Lyase
Gene Ontology (GO)
Biological_process	glyoxylate cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW citrate hydro-lyase (cis-aconitate-forming) activity Inferred from electronic annotation. Source: EC isocitrate hydro-lyase (cis-aconitate-forming) activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – 764	›764	Aconitate hydratase		PRO_0000076653
Regions
	Region	75 – 77	3	Substrate binding By similarity
	Region	648 – 649	2	Substrate binding By similarity
Sites
	Metal binding	307	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	372	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	375	1	Iron-sulfur (4Fe-4S) By similarity
	Binding site	405	1	Substrate By similarity
	Binding site	410	1	Substrate By similarity
	Binding site	568	1	Substrate By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q42669 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: E4A9B011FC6922F0	FASTA	764	83,274
	10 20 30 40 50 60 HEAKTENAVQ ANMELEFKRN RERFGFLKWG SSAFHNMLVV PPGSGIVHQV NLEYLGRVVF 70 80 90 100 110 120 NTNGLLYPDS VVGTDSHTTM IDGLGVAGWG VGGIEAEAAM LGQPMSMVLP GVVGFKLVGK 130 140 150 160 170 180 LRNGVTATDL VLTVTQMLRK HGVVGKFVEF YGEGMGELSL ADRATIANMS PEYGATMGFF 190 200 210 220 230 240 PVDHVTLQYL KLTGRKDETI SMIESYLLAN KMFVDYSEPQ VERVYSSHIE LNLSDVEPCI 250 260 270 280 290 300 SGPKRPHDRV PLKEMKADWH ACLDNRVGFK GFAIPKEAQV KVAEFNFHGS PAQLRHGDVV 310 320 330 340 350 360 IAAITSCTNT SSSVMLGAAL VAKKACELGL EVKPWIKTVL LQALGVVTKY LAKSGLQKYL 370 380 390 400 410 420 NQLGFNIVGY GCTTCIGNSG DIDESVASAI TGNDIVAAAV LSGNRNFEGR VHPLTRANYL 430 440 450 460 470 480 ASPPLVVAYA LAGTVDIDFE SEPIGVGKDG KKVFFRDIWP TSEEVAVVVN SNVLPDMFRA 490 500 510 520 530 540 TYQAITEGNA TWNLLSVPEG TLYSWDPTST YIHEPPYFKD MSMSPPGPHG VKNAYCLLNF 550 560 570 580 590 600 GDSITTDHIS PAGSIHKDSP AAKYLLERGV DRRDFNSYGV AVVMMRLWHV HFANIRIVNK 610 620 630 640 650 660 LLKGEVGPKT IHIPSREKLS VFDAAMRYKS EGQDTIILAG AEYGIGSSRD WAAKGPMLLG 670 680 690 700 710 720 VKAVIAKSFE RIHRSNLVGM GIIPLCFKAG EDADSLGLTG HERFTIDLPS NVGEIRPGQD 730 740 750 760 VAVVTDTGKS FSCILRFDTE VELAYFDHGG ILQYVIRNLI HSKH

References

[1]

"Structure, genomic organization, and expression of the Arabidopsis thaliana aconitase gene. Plant aconitase show significant homology with mammalian iron-responsive element-binding protein." Peyret P., Perez P., Alric M. J. Biol. Chem. 270:8131-8137(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Cantaloupe. Tissue: Fruit.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X82840 mRNA. Translation: CAA58047.1.
PIR	S49849.
3D structure databases
ProteinModelPortal	Q42669.
ModBase	Search...
Proteomic databases
ProMEX	Q42669.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00227.
Family and domain databases
Gene3D	3.20.19.10. 1 hit. 3.30.499.10. 3 hits. 3.40.1060.10. 1 hit.
InterPro	IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3. IPR015937. Acoase/IPM_deHydtase. IPR001030. Acoase/IPM_deHydtase_lsu_aba. IPR015928. Aconitase/3IPM_dehydase_swvl. IPR006249. Aconitase/Fe_reg_prot_2. IPR015934. Aconitase/Fe_reg_prot_2/AcnD. IPR015932. Aconitase/IPMdHydase_lsu_aba_2. IPR018136. Aconitase_4Fe-4S_BS. IPR000573. AconitaseA/IPMdHydase_ssu_swvl. [Graphical view]
PANTHER	PTHR11670. PTHR11670. 1 hit. PTHR11670:SF1. PTHR11670:SF1. 1 hit.
Pfam	PF00330. Aconitase. 1 hit. PF00694. Aconitase_C. 1 hit. [Graphical view]
PRINTS	PR00415. ACONITASE.
SUPFAM	SSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit. SSF53732. Aconitase_N. 1 hit.
TIGRFAMs	TIGR01341. aconitase_1. 1 hit.
PROSITE	PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACOC_CUCMC

Accession

Primary (citable) accession number: Q42669

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	April 3, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program