【目的】 本研究旨在丰富蜜蜂球囊菌Ascosphaera apis奎尼酸渗透酶（Quinate permease, AaqutD）的理化性质和分子特征信息，为深入开展AaqutD基因的功能研究提供科学依据。【方法】 通过PCR扩增AaqutD的编码序列（Coding sequence, CDS）并进行Sanger测序。使用相关软件预测AaqutD的理化性质、信号肽、磷酸化位点、二级结构、三级结构和蛋白互作网络。利用MEME软件和Batch CD-Search工具分别预测蜜蜂球囊菌和其他10种真菌qutD所含保守基序和结构域。通过Mega 11.0软件构建蜜蜂球囊菌和其他11种真菌qutD的系统进化树。采用RT-qPCR检测蜜蜂球囊菌侵染中华蜜蜂Apis cerana cerana工蜂幼虫过程中AaqutD的相对表达量。【结果】 成功克隆到AaqutD的CDS。AaqutD在蜜蜂球囊菌孢子中表达。AaqutD的分子量约为59.66 kD，分子式为C₂₇₆₂H₄₁₄₉N₆₈₉O₇₃₃S₂₉，脂溶系数为88.77，等电点为7.51，平均亲水系数为0.286。AaqutD可同时定位于内质网、线粒体和细胞核；AaqutD含有40个磷酸化位点，240个α-螺旋，111条延长链，29个β-转角，155个无规则卷曲，但不含典型的信号肽。AaqutD与模板A0A168DJE0.1.A之间的序列同源性为100%；AaqutD可能与肿瘤蛋白p73等10个蛋白互作。蜜蜂球囊菌和其他10种真菌的qutD皆包含1个相同的结构域（Sugartr）和11个相同的保守基序。蜜蜂球囊菌与针状球囊菌Ascosphaera acerosa的qutD在进化树上聚为一支。相较于接种后1 d（1 day post inoculation, 1 dpi），幼虫肠道中AaqutD的表达量在2 d和3 d均显著上调（P<0.05）。【结论】 AaqutD是一种潜在的亲水性和胞内蛋白，蜜蜂球囊菌和其他真菌的qutD具有较高的保守性与同源性，蜜蜂球囊菌与针状球囊菌球囊的qutD亲缘关系最高，AaqutD在蜜蜂球囊菌侵染中华蜜蜂工蜂幼虫的过程中被显著激活。

 [Aim]  To determine the physicochemical properties and molecular characteristics of the quinate permease gene (qutD) in the fungus Ascosphaera apis (AaqutD) and thereby provide a foundation for in-depth investigation of the function of this gene. [Methods]  The coding sequence (CDS) of AaqutD underwent PCR amplification and subsequent TA cloning. Predictions regarding its physicochemical properties, signal peptide, phosphorylation sites, secondary and tertiary structures, as well as protein interaction network, were made utilizing appropriate software tools. Conserved motifs and domains of this gene in As. apis and ten other fungi were forecasted through MEME software and the BatchCD-Search tool, respectively. Subsequently, a phylogenetic tree was constructed using Mega11.0 software. The relative expression of AaqutD in As. apis infecting worker larvae of Ap. cerana cerana was assessed using RT-qPCR. [Results]  The AaqutD CDS was successfully cloned. AaqutD was expressed in As. apis spores. The molecular weight of AaqutD is around 59.66 kD, with a molecular formula of C₂₇₆₂H₄₁₄₉N₆₈₉O₇₃₃S₂₉. It has a fat coefficient of 88.77, an isoelectric point of 7.51, and an average hydrophilicity coefficient of 0.286. AaqutD was simultaneously localized in the endoplasmic reticulum, mitochondria and nuclei. AaqutD has 40 phosphorylation sites, 240 α-helices, 111 extended chains, 29 β-turns and 155 irregular coils, however, it lacks a typical signal peptide. There is 100% sequence homology between AaqutD and the template A0A168DJE0.1.A. AaqutD may interact with 10 proteins including the tumor protein p73. The same structural domain (Sugartr) and the same eleven conserved motifs, were identified in qutD in As. apis and 10 other fungi. qutD of As. apis and Ap. acerosa clustered in one clade on the phylogenetic tree. Expression of AaqutD was significantly upregulated (P<0.05) 2- and 3-days post-inoculation (d) compared to that at 1 d. [Conclusion]  AaqutD is a potential hydrophilic and intracellular protein that is highly conserved and homologous with the qutD gene of other fungi. AaqutD is most closely related to the qutD gene of Ap. acerosa. AaqutD is significantly activated in As. apis during the infection of Ap. cerana cerana worker larvae.