{"doi":"10.1159/000085789","title":"Carbonic Anhydrases Fused to Anion Transporters of the SulP Family: Evidence for a Novel Type of Bicarbonate Transporter","abstract":"<jats:p>The sulfate permease (SulP) family of secondary carriers (TC #2.A.53) includes functionally characterized members that are inorganic anion:H&lt;sup&gt;+&lt;/sup&gt; symporters and anion:anion antiporters. We here describe members of this family that are fused to non-transporter domains, a relatively rare occurrence in prokaryotes. One subfamily includes members that are either fused to or are encoded within operons that also encode homologues of carbonic anhydrases, suggesting that these carriers function to take up bicarbonate or carbonate. Within another subfamily, a SulP homologue is fused to rhodanese, a thiosulfate:cyanide sulfotransferase, suggesting that this carrier functions in sulfate uptake. Some homologues are encoded in operons that also encode putative Na&lt;sup&gt;+&lt;/sup&gt;/H&lt;sup&gt;+&lt;/sup&gt; antiporters of the NhaD family (TC #2.A.62) or putative Na&lt;sup&gt;+&lt;/sup&gt;:HCO&lt;sub&gt;3&lt;/sub&gt;&lt;sup&gt;–&lt;/sup&gt; symporters of the SBT family (TC #2.A.83). SulP homologues present in fungi and some bacteria are fused to cyclic AMP-binding domains and STAS domains that presumably function in regulation or targeting. Phylogenetic analyses reveal the relationships of these proteins and protein domains to each other and show that in some cases, but not in others, the hydrophilic domains/proteins have coevolved with the transporters.</jats:p>","journal":"Microbial Physiology","year":2004,"id":627654,"datarank":0.6038027536102726,"base_score":4.02535169073515,"endowment":4.02535169073515,"self_citation_contribution":0.6038027536102726,"citation_network_contribution":0.0,"self_endowment_contribution":0.6038027536102726,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":55,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1624560,"name":"Milton H. Saier Jr.","orcid":null,"position":1,"is_corresponding":false},{"id":1624559,"name":"Jeremy Felce","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Carbonic Anhydrases Fused to Anion Transporters of the SulP Family: Evidence for a Novel Type of Bicarbonate Transporter","abstract":"<jats:p>The sulfate permease (SulP) family of secondary carriers (TC #2.A.53) includes functionally characterized members that are inorganic anion:H&lt;sup&gt;+&lt;/sup&gt; symporters and anion:anion antiporters. We here describe members of this family that are fused to non-transporter domains, a relatively rare occurrence in prokaryotes. One subfamily includes members that are either fused to or are encoded within operons that also encode homologues of carbonic anhydrases, suggesting that these carriers function to take up bicarbonate or carbonate. Within another subfamily, a SulP homologue is fused to rhodanese, a thiosulfate:cyanide sulfotransferase, suggesting that this carrier functions in sulfate uptake. Some homologues are encoded in operons that also encode putative Na&lt;sup&gt;+&lt;/sup&gt;/H&lt;sup&gt;+&lt;/sup&gt; antiporters of the NhaD family (TC #2.A.62) or putative Na&lt;sup&gt;+&lt;/sup&gt;:HCO&lt;sub&gt;3&lt;/sub&gt;&lt;sup&gt;–&lt;/sup&gt; symporters of the SBT family (TC #2.A.83). SulP homologues present in fungi and some bacteria are fused to cyclic AMP-binding domains and STAS domains that presumably function in regulation or targeting. Phylogenetic analyses reveal the relationships of these proteins and protein domains to each other and show that in some cases, but not in others, the hydrophilic domains/proteins have coevolved with the transporters.</jats:p>","is_dataset_classified":null,"base_score":4.02535169073515,"endowment":4.02535169073515,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"16088218","pmcid":null,"openalex_id":"https://openalex.org/W1991394745","authors":[],"funders":[{"funder_name":"NIGMS NIH HHS","grant_id":"GM55434","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"GM64368","title":null}],"total_grants":2,"fwci":1.988,"citation_percentile":0.87433027,"influential_citations":0,"citation_trend":[{"year":2012,"count":3},{"year":2013,"count":4},{"year":2014,"count":5},{"year":2015,"count":2},{"year":2016,"count":4},{"year":2017,"count":3},{"year":2019,"count":4},{"year":2020,"count":1},{"year":2023,"count":4},{"year":2024,"count":4}],"oa_status":"closed","license":"https://www.karger.com/Services/SiteLicenses","oa_locations":[{"url":"https://www.karger.com/Article/Pdf/85789","host_type":"publisher"},{"url":"https://doi.org/10.1159/000085789","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/16088218","host_type":"repository"}],"fields_of_study":["Cassava research and cyanide","Plant Stress Responses and Tolerance","Neonatal Health and Biochemistry","Anion Transport Proteins","Bacteria","Bicarbonates","Biological Transport","Carbonic Anhydrases","Computational Biology","Cyclic AMP","Gene Fusion","Hydrophobic and Hydrophilic Interactions","Phylogeny","Protein Binding","Protein Structure, Tertiary"],"mesh_terms":["Cyclic AMP","Bacteria","Bicarbonates","Biological Transport","Carbonic Anhydrases","Phylogeny","Protein Binding","Protein Structure, Tertiary","Computational Biology","Anion Transport Proteins","Gene Fusion","Hydrophobic and Hydrophilic Interactions"],"keywords":["Antiporters","Symporter","Operon","Subfamily","Biochemistry","Transporter","Solute carrier family","Bicarbonate","Chemistry","Rhodanese","Transmembrane protein","Protein family","Membrane transport protein","Permease","Biology","Gene","Escherichia coli","Enzyme"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Clean water and sanitation"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-04T18:21:09.663657Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}