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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O75027: Variant p.Glu433Lys

Iron-sulfur clusters transporter ABCB7, mitochondrial
Gene: ABCB7
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Variant information Variant position: help 433 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Glutamate (E) to Lysine (K) at position 433 (E433K, p.Glu433Lys). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from medium size and acidic (E) to large size and basic (K) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In ASAT; impaired maturation of cytosolic Fe/S proteins, loss of the ability to couple MgATP binding with stimulation of ATPase activity at the nucleotide binding domain;; loss of [2Fe-2S]-(GS)4 cluster transport. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 433 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 752 The length of the canonical sequence.
Location on the sequence: help VNGLLFQLSLPLNFLGTVYR E TRQALIDMNTLFTLLKVDTQ The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         VNGLLFQLSLPLNFLGTV--YRETRQALIDMNTLFTLLKVDTQ

Mouse                         VNGLLFQLSLPLNFLGTV--YRETRQALIDMNTLFTLLKVD

Rat                           VNGLLFQLSLPLNFLGTV--YRETRQALIDMNTLFTLLKVD

Zebrafish                     VNGLLFQLSLPLNFLGTV--YRETRQALIDMNTLFTLLSVD

Slime mold                    LQFILYSLMITASMNGLIGSINEIQKLISSSKRIFSLID--
Sequence annotation in neighborhood: help The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.
TypePositionsDescription
Chain 23 – 752 Iron-sulfur clusters transporter ABCB7, mitochondrial
Topological domain 431 – 752 Mitochondrial matrix
Domain 140 – 436 ABC transmembrane type-1
Binding site 428 – 428
Mutagenesis 433 – 433 E -> D. Significantly increases ATPase activity by [2Fe-2S]-(GS)4 cluster stimulation. Increases affinity for Mg-ATP. Does not affect affinity for Mg-ATP in the presence of the in the presence of [2Fe-2S]-(GS)4 cluster. Does not affect [2Fe-2S]-(GS)4 cluster transport.
Mutagenesis 433 – 433 E -> K. Loss of ATPase activity stimulation by [2Fe-2S]-(GS)4 cluster stimulation. Loss of the ability to couple MgATP binding with stimulation of ATPase activity at the nucleotide binding domain. Loss of [2Fe-2S]-(GS)4 cluster transport.
Mutagenesis 433 – 433 E -> Q. Loss of ATPase activity stimulation by [2Fe-2S]-(GS)4 cluster stimulation. Loss of the ability to couple MgATP binding with stimulation of ATPase activity at the nucleotide binding domain. Loss of [2Fe-2S]-(GS)4 cluster transport.



Literature citations
Human ABC7 transporter: gene structure and mutation causing X-linked sideroblastic anemia with ataxia with disruption of cytosolic iron-sulfur protein maturation.
Bekri S.; Kispal G.; Lange H.; Fitzsimons E.; Tolmie J.; Lill R.; Bishop D.F.;
Blood 96:3256-3264(2000)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANT ASAT LYS-433; Evolution of the human mitochondrial ABCB7 [2Fe-2S](GS)4 cluster exporter and the molecular mechanism of an E433K disease-causing mutation.
Pearson S.A.; Cowan J.A.;
Arch. Biochem. Biophys. 697:108661-108661(2021)
Cited for: ACTIVITY REGULATION; MUTAGENESIS OF GLU-433; BIOPHYSICOCHEMICAL PROPERTIES; FUNCTION; CATALYTIC ACTIVITY; CHARACTERIZATIONOF VARIANT ASAT LYS-433;
Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.