Reviewed, UniProtKB/Swiss-Prot Q0VCU1 (ACOC_BOVIN)

Names and origin

Protein names

Recommended name:
    Cytoplasmic aconitate hydratase
      Short name=Aconitase
    EC=4.2.1.3
Alternative name(s):
    Citrate hydro-lyase
    Iron-responsive element-binding protein 1
      Short name=IRE-BP 1

Gene names

Name:

ACO1

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	889 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Binds to iron-responsive elements (IRES), which are stem-loop structures found in the 5'-UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'-UTR of transferrin receptor mRNA. Binding to the IRE element in ferritin results in the repression of its mRNA translation. Binding of the protein to the transferrin receptor mRNA inhibits the degradation of this otherwise rapidly degraded mRNA By similarity. This protein also expresses aconitase activity By similarity.
Catalytic activity	Citrate = isocitrate.
Cofactor	Binds 1 4Fe-4S cluster per subunit By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the aconitase/IPM isomerase family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Cytoplasm
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding RNA-binding
Molecular function	Lyase
Gene Ontology (GO)
Biological process	tricarboxylic acid 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 RNA binding Inferred from electronic annotation. Source: UniProtKB-KW aconitate hydratase activity Inferred from electronic annotation. Source: EC iron 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 – 889	889	Cytoplasmic aconitate hydratase		PRO_0000285207
Sites
	Metal binding	437	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	503	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	506	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0VCU1-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 2BDD83B6294E6342	FASTA	889	98,204
	10 20 30 40 50 60 MSNPFAHLVE PLDPAQPGKK FFNLNKLEDS RYGSLPFSIR VLLEAAIRNC DQFLVKKNDV 70 80 90 100 110 120 ENILNWKVMQ HKNIEVPFKP ARVILQDFTG VPAVVDFAAM RDAVKKLGGN PEKINPICPA 130 140 150 160 170 180 DLVIDHSIQV DFNRRADSLK KNQDLEFERN KERFEFLKWG SQAFHNMRII PPGSGIIHQV 190 200 210 220 230 240 NLEYLARVVF DQDGYYYPDS LVGTDSHTTM IDGLGVLGWG VGGIEAEAVM LGQPISMVLP 250 260 270 280 290 300 QVIGYRLVGN PHPLVTSTDI VLTITKHLRQ VGVVGKFVEF FGPGVAQLSI ADRATIANMC 310 320 330 340 350 360 PEYGATAAFF PVDEVSIKYL VQTGRDKEKV KHIKQYLQAV GMFRDFSDSS QDPDFAQVVE 370 380 390 400 410 420 LDLKTVVPCC SGPKRPQDKV AVSDMKKDFE SCLGAKQGFK GFQVAPDHHN DHKTFIYNNS 430 440 450 460 470 480 KFTLAHGSVV IAAITSCTNT SNPSVMLGAG LLAKKAVDAG LSVKPYIKTS LSPGSGVVTY 490 500 510 520 530 540 YLRESGVMPY LSQLGFDVVG YGCMTCIGNS GPLPEAVVEA IVQGDLVAVG VLSGNRNFEG 550 560 570 580 590 600 RVHPNTRANY LASPPLVIAY AIAGTIRIDF EKEPLGVNAK GQQVFLKDIW PTRDEIQAVE 610 620 630 640 650 660 RQYVIPGMFK EVYQKIETVN ESWNALAAPS DKLYCWNPKS TYIKSPPFFE DLTLDLQPPK 670 680 690 700 710 720 SIVDAYVLLN LGDSVTTDHI SPAGNIARNS PAARYLTNRG LTPREFNSYG SRRGNDAIMA 730 740 750 760 770 780 RGTFANIRLL NKFLNKQAPQ TIHLPSGEIL DVFDAAERYQ QAGLPLIVLA GKEYGSGSSR 790 800 810 820 830 840 DWAAKGPFLL GIRAVLAESY ERIHRSNLVG MGVIPLEYLP GENADTLGLT GRERYTISIP 850 860 870 880 ETLKPRMKVQ IKLDTGKTFQ AVMRFDTDVE LTYFHNGGIL NYMIRKMTK

References

[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Fetal pons.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BC120006 mRNA. Translation: AAI20007.1.
IPI	IPI00685374.
RefSeq	NP_001069059.1.
UniGene	Bt.53789
3D structure databases
SMR	Q0VCU1. Positions 2-889.
ModBase	Search...
Genome annotation databases
Ensembl	ENSBTAG00000000555. Bos taurus. [Contig view]
GeneID	512995.
KEGG	bta:512995.
Phylogenomic databases
HOVERGEN	Q0VCU1.
Enzyme and pathway databases
BRENDA	4.2.1.3. 251.
Family and domain databases
InterPro	IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3. IPR001030. Acoase/IPM_deHydtase_lsu_aba. IPR015937. Aconitase-like_core. 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]
Gene3D	G3DSA:3.30.499.10. Acnase/IPM_dHydase_lsu_aba_1/3. 2 hits. G3DSA:3.20.19.10. Aconitase/3IPM_dehydase_swvl. 1 hit. G3DSA:3.40.1060.10. Aconitase/IPMdHydase_lsu_aba_2. 1 hit.
PANTHER	PTHR11670. Aconitase-like_core. 1 hit. PTHR11670:SF1. Aconitase/Fe_reg_prot_2/AcnD. 1 hit.
Pfam	PF00330. Aconitase. 1 hit. PF00694. Aconitase_C. 1 hit. [Graphical view]
PRINTS	PR00415. ACONITASE.
ProDom	PD000511. Aconitase_N. 1 hit. [Graphical view] [Entries sharing at least one domain]
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_BOVIN

Accession

Primary (citable) accession number: Q0VCU1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 2007
Last sequence update:	September 5, 2006
Last modified:	June 16, 2009
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)