SitesBLAST
Comparing WP_059153352.1 NCBI__GCF_001046635.1:WP_059153352.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 16 hits to proteins with known functional sites (download)
9cp8A Crystal structure of dhps-3-dehydrogenase, hpsn from cupriavidus pinatubonensis in complex with product (r-sulfolactate) and nadh (see paper)
47% identity, 96% coverage: 1:424/443 of query aligns to 1:422/436 of 9cp8A
- binding (2r)-3-sulfolactic acid: H126 (≠ L129), S226 (≠ T228), H251 (= H254), E318 (= E319), H319 (= H320), D352 (= D353), K353 (= K354), H359 (= H360)
- binding 1,4-dihydronicotinamide adenine dinucleotide: L45 (≠ F47), D46 (= D48), Y118 (= Y121), P120 (= P123), A121 (≠ G124), G122 (= G125), G177 (= G179), G178 (= G180), P201 (= P203), G202 (= G204), N203 (= N205), F205 (= F207), A223 (= A225), G224 (= G226), S226 (≠ T228), H251 (= H254), E318 (= E319), H359 (= H360), V360 (≠ T361), L361 (= L362)
- binding zinc ion: Q248 (= Q251), H251 (= H254), D352 (= D353)
9cp7A Crystal structure of dhps-3-dehydrogenase, hpsn from cupriavidus pinatubonensis in complex with product analogue (l-cysteate) and nadh (see paper)
47% identity, 96% coverage: 1:424/443 of query aligns to 1:422/436 of 9cp7A
- binding 1,4-dihydronicotinamide adenine dinucleotide: L45 (≠ F47), D46 (= D48), Y118 (= Y121), P120 (= P123), A121 (≠ G124), G122 (= G125), G177 (= G179), G178 (= G180), P201 (= P203), G202 (= G204), N203 (= N205), F205 (= F207), A223 (= A225), G224 (= G226), S226 (≠ T228), H251 (= H254), E318 (= E319), H359 (= H360), L361 (= L362)
- binding cysteinesulfonic acid: H126 (≠ L129), S226 (≠ T228), H251 (= H254), E318 (= E319), H319 (= H320), D352 (= D353), K353 (= K354), H359 (= H360), M408 (≠ F410), H411 (= H413)
- binding zinc ion: Q248 (= Q251), H251 (= H254), D352 (= D353)
9cp9A Sulfopropanediol 3-dehydrogenase (see paper)
47% identity, 95% coverage: 4:424/443 of query aligns to 3:421/435 of 9cp9A
- binding (2R)-2,3-dihydroxypropane-1-sulfonic acid: H125 (≠ L129), S225 (≠ T228), H250 (= H254), E317 (= E319), D351 (= D353), K352 (= K354), H358 (= H360)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D45 (= D48), Y117 (= Y121), P119 (= P123), A120 (≠ G124), G121 (= G125), G176 (= G179), G177 (= G180), P200 (= P203), G201 (= G204), N202 (= N205), F204 (= F207), A222 (= A225), G223 (= G226), S225 (≠ T228), H250 (= H254), E317 (= E319), H358 (= H360), V359 (≠ T361), L360 (= L362)
- binding zinc ion: Q247 (= Q251), H250 (= H254), D351 (= D353)
8v37A Crystal structure of hpsn d352a mutant from cupriavidus pinatubonensis in complex with NAD+ (see paper)
46% identity, 96% coverage: 1:424/443 of query aligns to 1:414/428 of 8v37A
8v36B Crystal structure of dhps-3-dehydrogenase, hpsn from cupriavidus pinatubonensis in complex with nadh (see paper)
44% identity, 92% coverage: 19:424/443 of query aligns to 6:388/402 of 8v36B
- binding 1,4-dihydronicotinamide adenine dinucleotide: L34 (≠ F47), D35 (= D48), Y107 (= Y121), G166 (= G179), G167 (= G180), Q169 (= Q182), P190 (= P203), G191 (= G204), N192 (= N205), F194 (= F207)
- binding zinc ion: H115 (≠ L129), Q227 (= Q251), H230 (= H254)
8v37B Crystal structure of hpsn d352a mutant from cupriavidus pinatubonensis in complex with NAD+ (see paper)
43% identity, 96% coverage: 1:424/443 of query aligns to 1:391/405 of 8v37B
4g09A The crystal structure of the c366s mutant of hdh from brucella suis in complex with a substituted benzyl ketone (see paper)
36% identity, 91% coverage: 18:421/443 of query aligns to 25:422/432 of 4g09A
- active site: Q253 (= Q251), H256 (= H254), E321 (= E319), H322 (= H320), D355 (= D353), H414 (= H413)
- binding (3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one: P126 (= P123), A130 (≠ Y127), Y132 (≠ L129), S134 (≠ A131), H256 (= H254), E321 (= E319), H322 (= H320), D355 (= D353), Y356 (≠ K354), H362 (= H360)
- binding zinc ion: H256 (= H254), D307 (≠ S305), D310 (≠ E308), D355 (= D353)
1kaeA L-histidinol dehydrogenase (hisd) structure complexed with l- histidinol (substrate), zinc and NAD (cofactor) (see paper)
36% identity, 91% coverage: 19:421/443 of query aligns to 34:427/434 of 1kaeA
- active site: Q259 (= Q251), H262 (= H254), E326 (= E319), H327 (= H320), D360 (= D353), H419 (= H413)
- binding L-histidinol: H262 (= H254), H327 (= H320), D360 (= D353), Y361 (≠ K354), H367 (= H360)
- binding nicotinamide-adenine-dinucleotide: F58 (= F47), Y130 (= Y121), P132 (= P123), P162 (= P153), G186 (= G180), P209 (= P203), G210 (= G204), N211 (= N205), F213 (= F207), H262 (= H254)
- binding zinc ion: Q259 (= Q251), H262 (= H254), D360 (= D353)
P06988 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Escherichia coli (strain K12) (see 2 papers)
36% identity, 91% coverage: 19:421/443 of query aligns to 34:427/434 of P06988
- Y130 (= Y121) binding NAD(+)
- Q188 (= Q182) binding NAD(+)
- N211 (= N205) binding NAD(+)
- Q259 (= Q251) binding Zn(2+)
- H262 (= H254) binding Zn(2+)
- D360 (= D353) binding Zn(2+)
- H419 (= H413) binding Zn(2+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1karA L-histidinol dehydrogenase (hisd) structure complexed with histamine (inhibitor), zinc and NAD (cofactor) (see paper)
36% identity, 91% coverage: 19:421/443 of query aligns to 31:424/431 of 1karA
- active site: Q256 (= Q251), H259 (= H254), E323 (= E319), H324 (= H320), D357 (= D353), H416 (= H413)
- binding histamine: S137 (≠ A131), H259 (= H254), D357 (= D353), Y358 (≠ K354), H364 (= H360)
- binding zinc ion: H259 (= H254), D357 (= D353)
1kahA L-histidinol dehydrogenase (hisd) structure complexed with l-histidine (product), zn and NAD (cofactor) (see paper)
36% identity, 91% coverage: 19:421/443 of query aligns to 31:424/431 of 1kahA
- active site: Q256 (= Q251), H259 (= H254), E323 (= E319), H324 (= H320), D357 (= D353), H416 (= H413)
- binding histidine: L135 (= L129), H259 (= H254), H324 (= H320), D357 (= D353), Y358 (≠ K354), H364 (= H360), E411 (= E408), L413 (≠ F410), H416 (= H413)
- binding zinc ion: H259 (= H254), D357 (= D353)
P10370 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
36% identity, 91% coverage: 19:421/443 of query aligns to 34:427/434 of P10370
- H99 (≠ A88) mutation to N: Slight decrease in activity.
- C117 (≠ L108) mutation C->A,S: Almost no change in activity.
- C154 (≠ V145) mutation C->A,S: Almost no change in activity.
- H262 (= H254) mutation to N: 7000-fold decrease in activity.
- H327 (= H320) mutation to N: 500-fold decrease in activity.
- H367 (= H360) mutation to N: Slight decrease in activity.
- H419 (= H413) mutation to Q: 20-fold decrease in activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6an0A Crystal structure of histidinol dehydrogenase from elizabethkingia anophelis
35% identity, 92% coverage: 21:426/443 of query aligns to 31:433/433 of 6an0A
- active site: Q260 (= Q251), H263 (= H254), E327 (= E319), H328 (= H320), D361 (= D353), H420 (= H413)
- binding histidine: E103 (≠ A93), N104 (≠ S94), K105 (≠ M95), R118 (≠ H110), E119 (≠ K111), A120 (≠ N112), K390 (≠ T382)
- binding zinc ion: H263 (= H254), D361 (= D353)
5vldF Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidine and NAD+ (see paper)
32% identity, 92% coverage: 21:429/443 of query aligns to 29:435/435 of 5vldF
- active site: Q258 (= Q251), H261 (= H254), E326 (= E319), H327 (= H320), D360 (= D353), H419 (= H413)
- binding histidine: S135 (≠ A131), S236 (≠ T228), Q258 (= Q251), H261 (= H254), E326 (= E319), H327 (= H320), D360 (= D353), Y361 (≠ K354), H367 (= H360), E414 (= E408), H419 (= H413)
- binding nicotinamide-adenine-dinucleotide: F55 (= F47), D56 (= D48), Y125 (= Y121), P127 (= P123), G129 (= G125), T130 (≠ K126), Q187 (= Q182), P208 (= P203), G209 (= G204), N210 (= N205), Y212 (≠ F207), A233 (= A225), G234 (= G226), S236 (≠ T228), H261 (= H254), E326 (= E319), H367 (= H360), V368 (≠ T361), L369 (= L362)
- binding zinc ion: Q258 (= Q251), H261 (= H254), D360 (= D353)
5vlbA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with imidazole (see paper)
32% identity, 92% coverage: 21:429/443 of query aligns to 28:434/434 of 5vlbA
5vlcA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidinol (see paper)
32% identity, 92% coverage: 21:427/443 of query aligns to 26:430/431 of 5vlcA
- active site: Q255 (= Q251), H258 (= H254), E323 (= E319), H324 (= H320), D357 (= D353), H416 (= H413)
- binding L-histidinol: H258 (= H254), E323 (= E319), H324 (= H320), D357 (= D353), Y358 (≠ K354), H364 (= H360), E411 (= E408), H416 (= H413)
- binding zinc ion: Q255 (= Q251), H258 (= H254), D357 (= D353)
Query Sequence
>WP_059153352.1 NCBI__GCF_001046635.1:WP_059153352.1
MAIYLKRGASAEAKATADRKVRDIVEAALADIEARGDAALREMSNRFDGWDRDDYRLSQA
EIEACVNNLSPQERKDIEFAQTQVRNFAKIQRASMTDVEVETLPGVVLGHKNIPLNSAGC
YVPGGKYPLLASAHMSVITAKVAGVKRVITCAPPFQGKPARAIVAAQAMAGADAIYALGG
IQAIGAMAIGTQTIEPVDILVGPGNAFVAEAKRQLFGRVGIDLFAGPTETLIIADEIGCD
PEMAATDILGQVEHGPDSPGVLLTNSEKFARATMAEIERLLEILPTADHAGKAWETFGEV
IVAESYEEMVRIADELASEHVQVMTADPDYFLQNMTNYGALFLGNRTNVSFGDKVIGTNH
TLPTKKAARYTGGLWVGKFLKTCTYQRVITDEASALIGEYCSRLCALEGFAGHGEQANIR
VRRFGGRDVPYAGQAEPTPQTTA
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory