P49608 (ACOC_CUCMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Aconitate hydratase, cytoplasmic Short name=Aconitase EC=4.2.1.3 Alternative name(s): Citrate hydro-lyase
Organism	Cucurbita maxima (Pumpkin) (Winter squash)
Taxonomic identifier	3661 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Cucurbitales › Cucurbitaceae › Cucurbiteae › Cucurbita

Protein attributes

Sequence length	898 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 – 898	898	Aconitate hydratase, cytoplasmic		PRO_0000076652
Regions
	Region	209 – 211	3	Substrate binding By similarity
	Region	784 – 785	2	Substrate binding By similarity
Sites
	Metal binding	441	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	507	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	510	1	Iron-sulfur (4Fe-4S) By similarity
	Binding site	90	1	Substrate By similarity
	Binding site	540	1	Substrate By similarity
	Binding site	545	1	Substrate By similarity
	Binding site	703	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P49608 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: ADFE73173CA54971	FASTA	898	98,005
	10 20 30 40 50 60 MAAENPFKEN LTSLPKPGGG EFGKYYSLPS LNDPRIDRLP YSIRILLESA IRNCDNFQVK 70 80 90 100 110 120 KEDVEKIIDW ENSSPKQVEI PFKPARVLLQ DFTGVPAVVD LACMRDAMNK LGSDSNKINP 130 140 150 160 170 180 LVPVDLVIDH SVQVDVARSE NAVQANMELE FQRNKERFAF LKWGSNAFQN MLVVPPGSGI 190 200 210 220 230 240 VHQVNLEYLG RVVFNTSGLL YPDSVVGTDS HTTMIDGLGV AGWGVGGIEA EAAMLGQPMS 250 260 270 280 290 300 MVLPGVVGFK LSGKLRNGVT ATDLVLTVTQ MLRKHGVVGK FVEFYGDGME ELSLADRATI 310 320 330 340 350 360 ANMSPEYGAT MGFFPVDHVT LQYLKLTGRS DETVSMIEAY LRANKMFVDY KEPQQEKVYS 370 380 390 400 410 420 SYLQLDLTDV EPCISGPKRP HDRVPLKEMK SDWHACLDNK VGFKGFAIPK EAQENVAKFS 430 440 450 460 470 480 FHGQPAELKH GSVVIAAITS CTNTSNPSVM LGAALVAKKA CELGLQVKPW VKTSLAPGSG 490 500 510 520 530 540 VVTKYLLKSG LQPYLNQQGF HIVGYGCTTC IGNSGDLDES VSAAISDNDI VAAAVLSGNR 550 560 570 580 590 600 NFEGRVHPLT RANYLASPPL VVAYALAGTV DIDFEKEPIG KGKDGKDVYF RDIWPSTEEI 610 620 630 640 650 660 AEVVQSSVLP DMFKSTYESI TKGNPMWNQL SVPSGTLYSW DPNSTYIHEP PYFKNMTMDP 670 680 690 700 710 720 PGAHGVKDAY CLLNFGDSIT TDHISPAGSI HKDSPAAKYL LERGVDRKDF NSYGSRRGND 730 740 750 760 770 780 EVMARGTFAN IRLVNKLLDG EVGPKTVHVP TGEKLSVFEA AEKYKSAGQD TIVLAGAEYG 790 800 810 820 830 840 SGSSRDWAAK GPMLLGVKAV IAKSFERIHR SNLVGMGIIP LCFKSGEDAD SLGLTGHERY 850 860 870 880 890 TIDLPDDISK IRPGQDVTVT TDSGKSFTCT VRFDTEVELA YFNNGGILPY VIRNLIKQ

References

[1]	"Cytosolic aconitase participates in the glyoxylate cycle in etiolated pumpkin cotyledons." Hayashi M., de Bellis L., Alpi A., Nishimura M. Plant Cell Physiol. 36:669-680(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Kurokawa Amakuri Nankin.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D29629 mRNA. Translation: BAA06108.1.
3D structure databases
ProteinModelPortal	P49608.
SMR	P49608. Positions 5-897.
ModBase	Search...
Proteomic databases
PRIDE	P49608.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
KEGG	dosa:Os03t0136900-01.
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_CUCMA

Accession

Primary (citable) accession number: P49608

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
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