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ACO1 aconitase 1 [ Bos taurus (domestic cattle) ]

Gene ID: 512995, updated on 4-Oct-2024

Summary

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Official Symbol
ACO1provided by VGNC
Official Full Name
aconitase 1provided by VGNC
Primary source
VGNC:VGNC:25545
See related
BGD:BT17803; Ensembl:ENSBTAG00000000555
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Bos taurus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos
Orthologs
human mouse all
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Genomic context

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See ACO1 in Genome Data Viewer
Location:
chromosome: 8
Exon count:
22
Annotation release Status Assembly Chr Location
RS_2023_09 current ARS-UCD2.0 (GCF_002263795.3) 8 NC_037335.1 (11611591..11674530, complement)

Chromosome 8 - NC_037335.1Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC100616098 Neighboring gene microRNA mir-2469 Neighboring gene TOP1 binding arginine/serine rich protein, E3 ubiquitin ligase Neighboring gene transfer RNA cysteine (anticodon ACA) Neighboring gene RNA sensor RIG-I Neighboring gene transfer RNA cysteine (anticodon ACA) Neighboring gene abl interactor 1-like

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_037335.1 Chromosome 8 Reference ARS-UCD2.0 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein. Kennedy MC, et al. Proc Natl Acad Sci U S A, 1992 Dec 15. PMID 1334546, Free PMC Article
  2. Cellular regulation of the iron-responsive element binding protein: disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding. Haile DJ, et al. Proc Natl Acad Sci U S A, 1992 Dec 15. PMID 1281544, Free PMC Article
  3. A whole-genome assembly of the domestic cow, Bos taurus. Zimin AV, et al. Genome Biol, 2009. PMID 19393038, Free PMC Article

GeneRIFs: Gene References Into Functions

Pathways from PubChem

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General gene information

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Homology

Clone Names

  • MGC140553

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables 3 iron, 4 sulfur cluster binding IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables 4 iron, 4 sulfur cluster binding IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables aconitate hydratase activity IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables iron-responsive element binding IEA
Inferred from Electronic Annotation
more info
 PubMed 
Process Evidence Code Pubs
involved_in citrate metabolic process IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in tricarboxylic acid cycle IEA
Inferred from Electronic Annotation
more info
 PubMed 
Component Evidence Code Pubs
located_in cytosol IEA
Inferred from Electronic Annotation
more info
 PubMed 
located_in mitochondrion IEA
Inferred from Electronic Annotation
more info
 PubMed 

General protein information

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Preferred Names
cytoplasmic aconitate hydratase
Names
IRE-BP 1
aconitase 1, soluble
citrate hydro-lyase
iron-responsive element-binding protein 1
NP_001069059.1
XP_005209909.1
XP_024851420.1

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_001075591.1 → NP_001069059.1  cytoplasmic aconitate hydratase

    See identical proteins and their annotated locations for NP_001069059.1

    Status: PROVISIONAL

    Source sequence(s)
    BC120006
    UniProtKB/Swiss-Prot
    Q0VCU1
    UniProtKB/TrEMBL
    F1MS05
    Related
    ENSBTAP00000000731.3, ENSBTAT00000000731.4
    Conserved Domains (3) summary
    cd01586
    Location:82 → 566
    AcnA_IRP; Aconitase A catalytic domain
    cd01580
    Location:670 → 839
    AcnA_IRP_Swivel; Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group ...
    PTZ00092
    Location:2 → 889
    PTZ00092; aconitate hydratase-like protein; Provisional

RefSeqs of Annotated Genomes: GCF_002263795.3-RS_2023_09

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference ARS-UCD2.0 Primary Assembly

Genomic

  1. NC_037335.1 Reference ARS-UCD2.0 Primary Assembly

    Range
    11611591..11674530 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_024995652.2 → XP_024851420.1  cytoplasmic aconitate hydratase isoform X2

    UniProtKB/TrEMBL
    A0A3Q1MHC4, F1MS05
    Related
    ENSBTAP00000070636.1, ENSBTAT00000075178.2
    Conserved Domains (1) summary
    cl28376
    Location:5 → 897
    AcnA; Aconitase A [Energy production and conversion]

  2. XM_005209852.5 → XP_005209909.1  cytoplasmic aconitate hydratase isoform X1

    UniProtKB/TrEMBL
    A0AAA9T160, F1MS05
    Related
    ENSBTAP00000091439.1, ENSBTAT00000100269.1
    Conserved Domains (3) summary
    cd01586
    Location:92 → 576
    AcnA_IRP; Aconitase A catalytic domain
    cd01580
    Location:680 → 849
    AcnA_IRP_Swivel; Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group ...
    PTZ00092
    Location:7 → 899
    PTZ00092; aconitate hydratase-like protein; Provisional
Nucleotide Protein Strain
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
Q0VCU1.1 GenPept UniProtKB/Swiss-Prot:Q0VCU1

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

Molecular Biology Databases
Research Materials