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AP is a multitype (e.g., PhoA, PhoD) family of hydrolases and is known as a promiscuous enzyme with broad DOP substrate compatibility. Yet, whether the multiple types differentiate on substrates and collaborate to provide physiological flexibility remain elusive. Here we identify PhoA and PhoDs and document the functional differentiation between PhoA and a PhoD (PhoD_45757) in <jats:italic>Phaeodactylum tricornutum<\/jats:italic>. CRISPR\/Cas9\u2010based mutations and physiological analyses reveal that (1) PhoA is a secreted enzyme and contributes the majority of total AP activity whereas PhoD_45757 is intracellular and contributes a minor fraction of the total AP activity, (2) AP gene expression compensates for each other after one is disrupted, (3) the DOP\u2192PhoA\u2192phosphate_uptake and the DOP_uptake\u2192PhoD\u2192phosphate pathways function interchangeably for some DOP substrates. These findings shed light on the underpinning of AP\u2019s multiformity and have important implications in phytoplankton phosphorus\u2010nutrient niche differentiation, physiological plasticity, and competitive strategy.<\/jats:p>","DOI":"10.1111\/mec.16475","type":"journal-article","created":{"date-parts":[[2022,4,21]],"date-time":"2022-04-21T07:09:45Z","timestamp":1650524985000},"page":"3389-3399","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":23,"title":["Functional differentiation and complementation of alkaline phosphatases and choreography of DOP scavenging in a marine diatom"],"prefix":"10.1111","volume":"31","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3816-4401","authenticated-orcid":false,"given":"Kaidian","family":"Zhang","sequence":"first","affiliation":[{"name":"State Key Laboratory of Marine Environmental Science and College of Ocean and Earth Sciences Xiamen University  Xiamen, Fujian 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