Comparing WP_007697503.1 NCBI__GCF_001277175.1:WP_007697503.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 6 hits to proteins with known functional sites (download)
P00946 Mannose-6-phosphate isomerase; Phosphohexomutase; Phosphomannose isomerase; PMI; EC 5.3.1.8 from Escherichia coli (strain K12) (see paper)
82% identity, 100% coverage: 1:391/392 of query aligns to 1:391/391 of P00946
3h1mA Crystal structure of mannose 6-phosphate isomerase (holo; zinc bound)
83% identity, 100% coverage: 1:391/392 of query aligns to 3:392/392 of 3h1mA
3h1yA Crystal structure of mannose 6-phosphate isomerase from salmonella typhimurium bound to substrate (f6p)and metal atom (zn)
83% identity, 100% coverage: 1:391/392 of query aligns to 3:391/391 of 3h1yA
P29952 Mannose-6-phosphate isomerase; Phosphohexomutase; Phosphomannose isomerase; PMI; EC 5.3.1.8 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
32% identity, 94% coverage: 3:370/392 of query aligns to 7:405/429 of P29952
Sites not aligning to the query:
5nw7A Crystal structure of candida albicans phosphomannose isomerase in complex with inhibitor (see paper)
36% identity, 73% coverage: 9:293/392 of query aligns to 13:322/440 of 5nw7A
P34948 Mannose-6-phosphate isomerase; Phosphohexomutase; Phosphomannose isomerase; PMI; EC 5.3.1.8 from Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) (see 2 papers)
36% identity, 73% coverage: 9:293/392 of query aligns to 14:323/441 of P34948
>WP_007697503.1 NCBI__GCF_001277175.1:WP_007697503.1
MQKLINSVQNYAWGSKTALTELYGVANPEGLPMAELWMGAHPKSSSKIQDAQGQTRALRE
VIEADKTALLGAPVAERFGELPFLFKVLCADQPLSIQVHPNKNASEDGFARENAAGIPLD
AAERNYKDPNHKPELVFALTPFLAMNAFREFSEIVSLLQPVAGAHTAIAHFLAEPNADRL
RDLFAGLLNMQGEEKSRALAVLKATVASQQGEPWDTIRFIAQFYPDDSGLFSPLLLNVVK
LNPGEAMFLFAETPHAYLQGVALEVMANSDNVLRAGLTPKYIDIPELVANVKFVAKPAGE
LLTQPEKDGAALEFPIPVEDFAFSLHDLHSQPQSLAQESAAILFCVEGEAVLSKGDERLS
LKPGESAFIAANESPVSVSGVGRLARVYNKLN
Or try a new SitesBLAST search
SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.
Lawrence Berkeley National Laboratory