P49609 (ACON_GRAGA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Aconitate hydratase, mitochondrial Short name=Aconitase EC=4.2.1.3 Alternative name(s): Citrate hydro-lyase
Organism	Gracilaria gracilis (Red alga)
Taxonomic identifier	2777 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Rhodophyta › Florideophyceae › Gracilariales › Gracilariaceae › Gracilaria

Protein attributes

Sequence length	779 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2.
Subunit structure	Monomer By similarity.
Subcellular location	Mitochondrion.
Sequence similarities	Belongs to the aconitase/IPM isomerase family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Lyase
Gene Ontology (GO)
Biological_process	tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	mitochondrion 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
	Transit peptide	1 – 28	28	Mitochondrion Potential
	Chain	29 – 779	751	Aconitate hydratase, mitochondrial		PRO_0000000548
Regions
	Region	190 – 192	3	Substrate binding By similarity
	Region	668 – 669	2	Substrate binding By similarity
Sites
	Metal binding	383	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	446	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	449	1	Iron-sulfur (4Fe-4S) By similarity
	Binding site	97	1	Substrate By similarity
	Binding site	472	1	Substrate By similarity
	Binding site	477	1	Substrate By similarity
	Binding site	605	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P49609 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 962173FFA8CBB836	FASTA	779	83,731
	10 20 30 40 50 60 MIAMDRIARI PIARWTSRAF RVSAAARQTP MSPLEAHNEL EPVYAAIDDR LNTVRSKLNR 70 80 90 100 110 120 PLTLAEKVLY GHLDDPERVP VRGETFLKLR PERVALQDAT AQMALIQFMA SARPQVAVPS 130 140 150 160 170 180 TIHCDHLIAA EVGAEEDMAK AKSQNKEVYD FLASAGAKYG LGFWKPGSGI IHQIVLENYA 190 200 210 220 230 240 FPGLLMIGTD SHTPNAGGLG ACAVGVGGAD AVDVMVGLPW ELKAPKVIGV KLTGKLQEWA 250 260 270 280 290 300 SPKDVILKVA GILTVKGGTG AIVEYFGEGV DSLSCTGMGT ICNMGAEIGA TTSMFPYNSR 310 320 330 340 350 360 MGDYLKATGR DGIASLADSF SEQLRADENA VYDQLIEINL SELEPHINGP FTPDLAHPLS 370 380 390 400 410 420 KFKEEVEKNG WPAELTVGLI GSCTNSSYED MARSASVVKQ ALSHGVKSKS IFNITPGSEQ 430 440 450 460 470 480 VRATISRDGI LDTFTEAGGT VLANACGPCI GQWNRSDVPK GTPNSIITSF NRNFSQRNDG 490 500 510 520 530 540 NPQTHAFVAS PEIVTAMSLA GSLKFNPATD SLQGADGAEF KLAAPSGDEL PVMGFDPGED 550 560 570 580 590 600 TFQPPSDDST SILVQIDPDS QRLSFLEPFP AWDGKDYTDM PVLIKARGKC TTDHISMAGP 610 620 630 640 650 660 WLKFRGHLDN ISNNMLIGAV NDENGEINNV KNAVTGEYGT VPDTARAYKA EGVKWVVIGD 670 680 690 700 710 720 ENYGEGSSRE HAALEPRHLG GVAVIVKSFA RIHETNLKKQ GMLPLTFNNP ADYDKIDSSD 730 740 750 760 770 KVSLVGLKNL TPGEPVTMTV TKADGTSMDI LLNHTFNDEQ LEWFRAGSAL NKIKIDLGT

References

[1]	"Characterization of the nuclear gene encoding mitochondrial aconitase in the marine red alga Gracilaria verrucosa." Zhou Y.H., Ragan M.A. Plant Mol. Biol. 28:635-646(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	U17709 Genomic DNA. Translation: AAA80494.1.
PIR	S57805.
3D structure databases
ProteinModelPortal	P49609.
SMR	P49609. Positions 28-774.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00223; UER00718.
Family and domain databases
Gene3D	3.20.19.10. 1 hit. 3.30.499.10. 2 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. IPR015932. Aconitase/IPMdHydase_lsu_aba_2. IPR018136. Aconitase_4Fe-4S_BS. IPR006248. Aconitase_mito-like. IPR000573. AconitaseA/IPMdHydase_ssu_swvl. [Graphical view]
PANTHER	PTHR11670. PTHR11670. 1 hit. PTHR11670:SF5. PTHR11670:SF5. 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	TIGR01340. aconitase_mito. 1 hit.
PROSITE	PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACON_GRAGA

Accession

Primary (citable) accession number: P49609

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)