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Majority of the bacterial HNOB domain proteins are predicted to covalently bind heme.
Because the middle domain of the SGCs is always associated with the HNOB domains (see below), we named it the HNOBA ( HNOB A ssociated) domain.
In order to test this further, we used a multiple alignment of the HNOB domain (Fig.
Though SGC α-subunits lack the histidine, the region encompassing the HNOB domain in human SGC1α has been shown to be important for functional heme binding by the dimeric enzyme [ 28 ] . Hence, in addition to covalent heme binding, HNOB domains may also interact with it non-covalently.
Thus, even in the bacteria, the HNOBA domain always appears to function in association with the HNOB domain.