Comparing BWI76_RS13295 FitnessBrowser__Koxy:BWI76_RS13295 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 5 hits to proteins with known functional sites (download)
2rjbA Crystal structure of uncharacterized protein ydcj (sf1787) from shigella flexneri which includes domain duf1338. Northeast structural genomics consortium target sfr276
79% identity, 100% coverage: 2:446/447 of query aligns to 1:418/418 of 2rjbA
2rjbD Crystal structure of uncharacterized protein ydcj (sf1787) from shigella flexneri which includes domain duf1338. Northeast structural genomics consortium target sfr276
73% identity, 97% coverage: 5:438/447 of query aligns to 1:372/372 of 2rjbD
2rjbC Crystal structure of uncharacterized protein ydcj (sf1787) from shigella flexneri which includes domain duf1338. Northeast structural genomics consortium target sfr276
70% identity, 99% coverage: 5:446/447 of query aligns to 1:364/364 of 2rjbC
Q88CC1 2-oxoadipate dioxygenase/decarboxylase; 2-hydroxyglutarate synthase; EC 1.13.11.93 from Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) (see paper)
60% identity, 98% coverage: 5:444/447 of query aligns to 7:455/464 of Q88CC1
6w1hA Crystal structure of the hydroxyglutarate synthase in complex with 2- oxoadipate from pseudomonas putida (see paper)
59% identity, 99% coverage: 5:445/447 of query aligns to 5:445/450 of 6w1hA
>BWI76_RS13295 FitnessBrowser__Koxy:BWI76_RS13295
MANTITADEIRESFSQAMSAMYQQEVPQYGTLLELVADVNLAILENNPTLHEQLANADEL
ARLNVERHGAIRVGTAEELATLRRMFAIMGMYPVSYYDLSQAGVPVHSTAFRPIDDAALA
RNPFRVFTSLLRLELIADEALRKRAAEILARRDIFTSRCRELIALHEQKGEFTAAEAREF
VQQALETFRWHRHATVDEETYHALHEEHRLIADVVCFPGCHINHLTPRTLDIDRVQALMP
ECGIAPKALIEGPPRRDVPILLRQTSFKALEEPVMFAGEHRGTHTARFGEIEQRGIALTP
KGRALYDRLLSEAGVGKDNLNHQRHLQEVFSPFPDSEFLLRQQGLAYFRYRLTPAGEAHR
QAFRPGDDPQPLIERGWVIAQPIIYEDFLPVSAAGIFQSNLGNEIQARSHGNASREAFEE
ALGCAVYDEFALYQQAEERSKRRCGLL
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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