SitesBLAST
Comparing AO353_15690 AO353_15690 formate dehydrogenase 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 20 (the maximum) hits to proteins with known functional sites (download)
6tg9A Cryo-em structure of nadh reduced form of NAD+-dependent formate dehydrogenase from rhodobacter capsulatus (see paper)
67% identity, 97% coverage: 12:944/962 of query aligns to 8:948/949 of 6tg9A
- active site: K289 (= K285), C380 (= C376), H381 (= H377), L545 (= L541), G582 (= G578), Q583 (= Q579)
- binding fe2/s2 (inorganic) cluster: C51 (= C56), V59 (≠ F64), G60 (= G65), C62 (= C67), C65 (= C70), C79 (= C84)
- binding 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraaza-anthracen-4-one guanosine dinucleotide: C255 (= C251), K289 (= K285), R351 (= R347), C352 (= C348), C380 (= C376), G414 (= G410), A415 (= A411), D419 (= D415), G420 (≠ A416), H421 (= H417), P443 (= P439), R444 (= R440), P464 (= P460), N467 (= N463), L545 (= L541), G546 (= G542), H550 (= H546), G582 (= G578), Q583 (= Q579), Q583 (= Q579), G649 (= G645), E650 (= E646), S655 (= S651), N680 (= N676), S693 (= S689), K698 (= K694), D724 (= D720), T820 (= T816), T821 (= T817), R823 (= R819), R823 (= R819), I824 (= I820), L825 (= L821), N829 (= N825), V830 (= V826), Q833 (= Q829), N902 (= N898), Y918 (= Y914), K919 (= K915)
- binding iron/sulfur cluster: H111 (= H116), C115 (= C120), C118 (= C123), A120 (= A125), C124 (= C129), C176 (= C171), I177 (= I172), V178 (= V173), C179 (= C174), M180 (≠ N175), C182 (= C177), C186 (= C181), I206 (≠ V201), C218 (= C214), S220 (= S216), C221 (= C217), G222 (= G218), C224 (= C220), C228 (= C224), T230 (= T226), A231 (= A227), C252 (= C248), Y254 (= Y250), C255 (= C251), V257 (= V253), C259 (= C255), F261 (= F257), C287 (= C283), K289 (= K285), V423 (= V419)
7vw6A Cryo-em structure of formate dehydrogenase 1 from methylorubrum extorquens am1 (see paper)
36% identity, 93% coverage: 24:921/962 of query aligns to 2:910/913 of 7vw6A
- binding fe2/s2 (inorganic) cluster: H32 (≠ K54), C34 (= C56), H35 (vs. gap), G45 (= G65), C47 (= C67), R48 (= R68), C50 (= C70), C64 (= C84)
- binding 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraaza-anthracen-4-one guanosine dinucleotide: K263 (= K285), K339 (≠ R347), C364 (= C372), C368 (= C376), G402 (= G410), N404 (= N412), N408 (≠ A416), D431 (= D438), P432 (= P439), R433 (= R440), F447 (≠ L458), G450 (= G461), D452 (≠ N463), G525 (= G540), M526 (≠ L541), G527 (= G542), Q530 (≠ E545), H531 (= H546), G563 (= G578), Q564 (= Q579), G630 (= G645), N632 (≠ D647), S636 (= S651), Q656 (= Q671), D657 (= D672), L658 (≠ I673), T805 (= T817), R807 (= R819), R807 (= R819), V808 (≠ I820), L809 (= L821), H811 (≠ Q823), W812 (≠ Y824), H813 (≠ N825), H813 (≠ N825), T814 (≠ V826), M817 (≠ Q829), F879 (= F890), N887 (= N898), F903 (≠ Y914), K904 (= K915)
- binding iron/sulfur cluster: C145 (= C171), I146 (= I172), Q147 (≠ V173), C148 (= C174), N149 (= N175), C151 (= C177), C155 (= C181), N161 (≠ T187), V163 (≠ A189), I164 (≠ L190), V175 (= V201), C188 (= C214), V189 (= V215), A190 (≠ S216), C191 (= C217), G192 (= G218), C194 (= C220), C198 (= C224), P199 (= P225), T200 (= T226), A202 (≠ T228), L203 (= L229), C227 (= C248), C230 (= C251), C234 (= C255), C261 (= C283), K263 (= K285), G264 (= G286), V411 (= V419)
1fdiA Oxidized form of formate dehydrogenase h from e. Coli complexed with the inhibitor nitrite (see paper)
37% identity, 74% coverage: 243:954/962 of query aligns to 3:715/715 of 1fdiA
- active site: C11 (= C251), L41 (≠ S282), C42 (= C283), K44 (= K285), S108 (= S345), R110 (= R347), D134 (= D370), C140 (= C376), H141 (= H377), S180 (≠ A416), M297 (≠ L541), R333 (= R577), G334 (= G578), Q335 (= Q579)
- binding 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraaza-anthracen-4-one guanosine dinucleotide: K44 (= K285), R110 (= R347), G111 (≠ C348), V139 (= V375), C140 (= C376), F173 (≠ M409), G174 (= G410), Y175 (≠ A411), N176 (= N412), D179 (= D415), S180 (≠ A416), C201 (≠ I437), D202 (= D438), P203 (= P439), R204 (= R440), L218 (= L458), G221 (= G461), N223 (= N463), G296 (= G540), M297 (≠ L541), G298 (= G542), F302 (≠ H546), G334 (= G578), Q335 (= Q579), Q335 (= Q579), G402 (= G645), E403 (= E646), T408 (≠ S651), Q428 (= Q671), D429 (= D672), I430 (= I673), S445 (≠ G688), D478 (= D720), T579 (= T817), V580 (≠ G818), R581 (= R819), R581 (= R819), E582 (≠ I820), H585 (≠ Q823), Y586 (= Y824), S587 (≠ N825), C588 (≠ V826), Y654 (≠ F890), N662 (= N898), Y678 (= Y914), K679 (= K915)
- binding nitrite ion: C140 (= C376), H141 (= H377), R333 (= R577), G334 (= G578), V338 (= V582)
- binding iron/sulfur cluster: C8 (= C248), Y10 (= Y250), C11 (= C251), S13 (≠ V253), C15 (= C255), L41 (≠ S282), C42 (= C283), K44 (= K285), P182 (= P418), I183 (≠ V419)
P07658 Formate dehydrogenase H; Formate dehydrogenase-H subunit alpha; FDH-H; Formate-hydrogen-lyase-linked, selenocysteine-containing polypeptide; EC 1.17.98.4 from Escherichia coli (strain K12) (see 2 papers)
37% identity, 74% coverage: 243:954/962 of query aligns to 3:715/715 of P07658
- C8 (= C248) binding
- Y10 (= Y250) binding
- C11 (= C251) binding
- C15 (= C255) binding
- C42 (= C283) binding
- K44 (= K285) binding
- U140 (≠ C376) modified: nonstandard, Selenocysteine
- M297 (≠ L541) binding
- Q301 (≠ E545) binding
- Q335 (= Q579) binding
- S445 (≠ G688) binding
- D478 (= D720) binding
- C588 (≠ V826) binding
- Y654 (≠ F890) binding
- Q655 (≠ H891) binding
- Y678 (= Y914) binding
- K679 (= K915) binding
2iv2X Reinterpretation of reduced form of formate dehydrogenase h from e. Coli (see paper)
36% identity, 74% coverage: 243:954/962 of query aligns to 3:697/697 of 2iv2X
- active site: C11 (= C251), L41 (≠ S282), C42 (= C283), K44 (= K285), S108 (= S345), C140 (= C376), H141 (= H377), S180 (≠ A416), M297 (≠ L541), R333 (= R577), G334 (= G578), Q335 (= Q579)
- binding guanylate-o'-phosphoric acidmono-(2-amino-5,6-dimercapto-4-oxo-3,5,6,7,8a,9,10,10a-octahydro-4h-8-oxa-1,3,9,10-tetraaza-anthracen-7-ylmethyl) ester: R110 (= R347), G111 (≠ C348), T112 (= T349), A137 (= A373), Q335 (= Q579), G402 (= G645), E403 (= E646), D404 (= D647), T408 (≠ S651), A410 (≠ P653), Q428 (= Q671), D429 (= D672), I430 (= I673), S445 (≠ G688), D478 (= D720), C588 (≠ V826), Y660 (= Y914)
- binding 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraaza-anthracen-4-one guanosine dinucleotide: K44 (= K285), F173 (≠ M409), G174 (= G410), Y175 (≠ A411), N176 (= N412), D179 (= D415), S180 (≠ A416), D202 (= D438), P203 (= P439), R204 (= R440), N223 (= N463), G296 (= G540), M297 (≠ L541), F302 (≠ H546), G334 (= G578), R581 (= R819), E582 (≠ I820), V583 (≠ L821), H585 (≠ Q823), Y586 (= Y824), S587 (≠ N825), K661 (= K915)
- binding iron/sulfur cluster: C8 (= C248), C11 (= C251), S13 (≠ V253), C15 (= C255), L41 (≠ S282), C42 (= C283), K44 (= K285), G45 (= G286), I183 (≠ V419)
7qv7S Cryo-em structure of hydrogen-dependent co2 reductase. (see paper)
39% identity, 60% coverage: 241:818/962 of query aligns to 1:571/571 of 7qv7S
7bkbD Formate dehydrogenase - heterodisulfide reductase - formylmethanofuran dehydrogenase complex from methanospirillum hungatei (hexameric, composite structure) (see paper)
37% identity, 58% coverage: 244:802/962 of query aligns to 7:548/549 of 7bkbD
2jiqA A new catalytic mechanism of periplasmic nitrate reductase from desulfovibrio desulfuricans atcc 27774 from crystallographic and epr data and based on detailed analysis of the sixth ligand (see paper)
30% identity, 71% coverage: 239:923/962 of query aligns to 1:719/720 of 2jiqA
- active site: K46 (= K285), S106 (= S345), C137 (= C376), M138 (≠ H377), A177 (= A416), M305 (≠ L541), T341 (≠ R577), G342 (= G578), Q343 (= Q579)
- binding 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraaza-anthracen-4-one guanosine dinucleotide: R11 (≠ A249), Q108 (≠ R347), C137 (= C376), G171 (= G410), S172 (≠ A411), E176 (≠ D415), A177 (= A416), D201 (= D438), P202 (= P439), R203 (= R440), P219 (= P460), D222 (≠ N463), C304 (≠ G540), M305 (≠ L541), G306 (= G542), Q309 (≠ E545), R310 (≠ H546), G342 (= G578), Q343 (= Q579), Q343 (= Q579), E413 (≠ G645), T414 (≠ E646), N415 (≠ D647), T419 (≠ S651), I440 (≠ Q671), E441 (≠ D672), F443 (= F674), P458 (≠ G688), F460 (≠ S690), S612 (≠ T817), M613 (≠ G818), R614 (= R819), R614 (= R819), I616 (≠ L821), H618 (≠ Q823), W619 (≠ Y824), H620 (≠ N825), H620 (≠ N825), T621 (≠ V826), T623 (≠ A828), F686 (= F890), N694 (= N898), Y710 (= Y914), K711 (= K915)
- binding nitrate ion: M251 (≠ I485), K583 (vs. gap), V589 (≠ R794), W591 (≠ M796), R593 (≠ T798), V704 (≠ A908)
- binding iron/sulfur cluster: C10 (= C248), C13 (= C251), T15 (≠ V253), C17 (= C255), L43 (≠ S282), C44 (= C283), V180 (= V419)
P81186 Periplasmic nitrate reductase; EC 1.9.6.1 from Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB) (see 3 papers)
30% identity, 71% coverage: 239:923/962 of query aligns to 36:754/755 of P81186
Sites not aligning to the query:
- 1:32 signal peptide, Tat-type signal
2jirA A new catalytic mechanism of periplasmic nitrate reductase from desulfovibrio desulfuricans atcc 27774 from crystallographic and epr data and based on detailed analysis of the sixth ligand (see paper)
30% identity, 71% coverage: 239:923/962 of query aligns to 1:719/720 of 2jirA
- active site: K46 (= K285), S106 (= S345), C137 (= C376), M138 (≠ H377), A177 (= A416), M305 (≠ L541), T341 (≠ R577), G342 (= G578), Q343 (= Q579)
- binding 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraaza-anthracen-4-one guanosine dinucleotide: R11 (≠ A249), K46 (= K285), Q108 (≠ R347), C137 (= C376), G171 (= G410), S172 (≠ A411), N173 (= N412), E176 (≠ D415), A177 (= A416), D201 (= D438), P202 (= P439), R203 (= R440), F217 (≠ L458), D222 (≠ N463), C304 (≠ G540), M305 (≠ L541), G306 (= G542), Q309 (≠ E545), R310 (≠ H546), G342 (= G578), Q343 (= Q579), Q343 (= Q579), E413 (≠ G645), T414 (≠ E646), N415 (≠ D647), T419 (≠ S651), I440 (≠ Q671), E441 (≠ D672), A442 (≠ I673), P458 (≠ G688), F460 (≠ S690), S612 (≠ T817), M613 (≠ G818), R614 (= R819), R614 (= R819), I616 (≠ L821), H618 (≠ Q823), W619 (≠ Y824), H620 (≠ N825), H620 (≠ N825), T621 (≠ V826), T623 (≠ A828), F686 (= F890), N694 (= N898), Y710 (= Y914), K711 (= K915)
- binding nitrite ion: V615 (≠ I820), F686 (= F890)
- binding iron/sulfur cluster: C10 (= C248), C13 (= C251), T15 (≠ V253), C17 (= C255), L43 (≠ S282), C44 (= C283), P179 (= P418), V180 (= V419)
2v45A A new catalytic mechanism of periplasmic nitrate reductase from desulfovibrio desulfuricans atcc 27774 from crystallographic and epr data and based on detailed analysis of the sixth ligand (see paper)
30% identity, 71% coverage: 239:923/962 of query aligns to 4:722/723 of 2v45A
- active site: K49 (= K285), S109 (= S345), C140 (= C376), M141 (≠ H377), A180 (= A416), M308 (≠ L541), T344 (≠ R577), G345 (= G578), Q346 (= Q579)
- binding 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraaza-anthracen-4-one guanosine dinucleotide: R14 (≠ A249), K49 (= K285), Q111 (≠ R347), C140 (= C376), G174 (= G410), N176 (= N412), E179 (≠ D415), A180 (= A416), D204 (= D438), P205 (= P439), R206 (= R440), P222 (= P460), D225 (≠ N463), C307 (≠ G540), M308 (≠ L541), G309 (= G542), Q312 (≠ E545), R313 (≠ H546), G345 (= G578), Q346 (= Q579), Q346 (= Q579), E416 (≠ G645), T417 (≠ E646), N418 (≠ D647), T422 (≠ S651), I443 (≠ Q671), E444 (≠ D672), A445 (≠ I673), F446 (= F674), P461 (≠ G688), F463 (≠ S690), S615 (≠ T817), M616 (≠ G818), R617 (= R819), R617 (= R819), V618 (≠ I820), I619 (≠ L821), H621 (≠ Q823), W622 (≠ Y824), H623 (≠ N825), H623 (≠ N825), T624 (≠ V826), T626 (≠ A828), F689 (= F890), N697 (= N898), Y713 (= Y914), K714 (= K915)
- binding iron/sulfur cluster: C13 (= C248), C16 (= C251), T18 (≠ V253), C20 (= C255), L46 (≠ S282), C47 (= C283), V183 (= V419)
7t30A Structure of electron bifurcating ni-fe hydrogenase complex hydabcsl in fmn/NAD(h) bound state (see paper)
27% identity, 72% coverage: 23:716/962 of query aligns to 3:620/666 of 7t30A
- binding fe2/s2 (inorganic) cluster: C36 (= C56), G45 (= G65), C47 (= C67), R48 (= R68), C50 (= C70), C64 (= C84)
- binding iron/sulfur cluster: F93 (≠ I113), H98 (≠ L118), F99 (≠ D119), C100 (= C120), C103 (= C123), Q105 (≠ A125), C109 (= C129), L141 (≠ F164), R147 (≠ K170), C148 (= C171), L150 (≠ V173), C151 (= C174), Q152 (≠ N175), C154 (= C177), C158 (= C181), C192 (= C214), V193 (= V215), N194 (≠ S216), C195 (= C217), G196 (= G218), A197 (= A219), C198 (= C220), C202 (= C224), P203 (= P225), T204 (= T226), G205 (≠ A227), T206 (= T228), I207 (≠ L229), C229 (= C248), C232 (= C251), G235 (= G254), C236 (= C255), L263 (≠ S282), C264 (= C283), V396 (= V419)
8oh5C Cryo-em structure of the electron bifurcating transhydrogenase stnabc complex from sporomusa ovata (state 2) (see paper)
29% identity, 68% coverage: 120:773/962 of query aligns to 562:1125/1172 of 8oh5C
- binding iron/sulfur cluster: C562 (= C120), L563 (= L121), C565 (= C123), C567 (≠ A125), C573 (≠ L131), C613 (= C171), V614 (≠ I172), L615 (≠ V173), C616 (= C174), G617 (≠ N175), C619 (= C177), C623 (= C181), I643 (≠ V201), C656 (= C214), I657 (≠ V215), S658 (= S216), C659 (= C217), G660 (= G218), C662 (= C220), C666 (= C224), G669 (≠ A227), A670 (≠ T228), C692 (= C248), Y694 (= Y250), C695 (= C251), C699 (= C255), C725 (= C283), R727 (≠ K285), G728 (= G286), V853 (= V419)
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 199, 201, 202, 203, 222, 223, 229, 230, 235, 239, 264, 265, 285, 288, 332, 471, 477, 479
- binding fe2/s2 (inorganic) cluster: 36, 45, 47, 48, 50, 64
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: 330, 331, 332, 333, 353, 354, 355, 432, 433, 434, 477
- binding iron/sulfur cluster: 96, 98, 100, 102, 104, 108, 147, 149, 151, 155, 156, 164, 170, 480
P33937 Periplasmic nitrate reductase; EC 1.9.6.1 from Escherichia coli (strain K12) (see 3 papers)
26% identity, 70% coverage: 248:924/962 of query aligns to 46:828/828 of P33937
- C46 (= C248) binding
- C49 (= C251) binding
- C53 (= C255) binding
- C81 (= C283) binding
- K83 (= K285) binding
- Q150 (≠ R347) binding
- N175 (≠ C372) binding
- C179 (= C376) binding
- 212:219 (vs. 409:416, 38% identical) binding
- STYQH 243:247 (≠ IVIDP 435:439) binding
- QSD 262:264 (≠ GTN 461:463) binding
- M372 (≠ L541) binding
- Q376 (≠ E545) binding
- N482 (≠ D647) binding
- SD 508:509 (≠ QD 671:672) binding
- K531 (= K694) binding
- D558 (vs. gap) binding
- 718:727 (vs. 817:826, 40% identical) binding
- N802 (= N898) binding
- K819 (= K915) binding
Sites not aligning to the query:
- 1:36 signal peptide, Tat-type signal
- 6 R→Q: Impairs interaction with NapD. Lack of nitrate reductase activity. Tat transport is blocked.
- 10 K→Q: Impairs interaction with NapD. Slight decrease in nitrate reductase activity. Minor defect in Tat transport.
- 17 A→L: Impairs interaction with NapD.; A→Q: Impairs interaction with NapD. Decrease in nitrate reductase activity. Defect in Tat transport.
2nyaA Crystal structure of the periplasmic nitrate reductase (nap) from escherichia coli (see paper)
26% identity, 70% coverage: 248:923/962 of query aligns to 10:791/791 of 2nyaA
- active site: N44 (≠ S282), C45 (= C283), K47 (= K285), C143 (= C376), M144 (≠ H377), M183 (≠ A416), M336 (≠ L541), T372 (≠ R577), G373 (= G578), Q374 (= Q579)
- binding 2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraaza-anthracen-4-one guanosine dinucleotide: R11 (≠ A249), K47 (= K285), Q114 (≠ R347), N139 (≠ C372), C143 (= C376), W176 (≠ M409), G177 (= G410), M183 (≠ A416), S207 (≠ I435), T208 (≠ V436), Y209 (≠ I437), F223 (≠ L458), D228 (≠ N463), T335 (≠ G540), M336 (≠ L541), M336 (≠ L541), G337 (= G542), F338 (≠ V543), Q340 (≠ E545), G373 (= G578), Q374 (= Q579), Q374 (= Q579), C444 (≠ G645), T445 (≠ E646), N446 (≠ D647), A450 (≠ S651), S472 (≠ Q671), D473 (= D672), P474 (≠ I673), T489 (≠ G688), A490 (≠ S689), M491 (≠ S690), K495 (= K694), D522 (vs. gap), T682 (= T817), G683 (= G818), R684 (= R819), R684 (= R819), L686 (= L821), H688 (≠ Q823), W689 (≠ Y824), H690 (≠ N825), H690 (≠ N825), T691 (≠ V826), S693 (≠ A828), F758 (= F890), N766 (= N898), F782 (≠ Y914), K783 (= K915), K784 (≠ V916)
- binding iron/sulfur cluster: C10 (= C248), C13 (= C251), C17 (= C255), C45 (= C283), I186 (≠ V419)
8e9hG Mycobacterial respiratory complex i, fully-inserted quinone (see paper)
26% identity, 71% coverage: 24:704/962 of query aligns to 5:612/782 of 8e9hG
- binding fe2/s2 (inorganic) cluster: R35 (≠ K54), C37 (= C56), D38 (≠ A57), G46 (= G65), C48 (= C67), R49 (= R68), C51 (= C70), A63 (= A82), C65 (= C84)
- binding guanosine-5'-triphosphate: R320 (= R347), R486 (≠ G564), R487 (≠ N565), G554 (= G645), E556 (≠ D647), D559 (≠ Q650), L579 (≠ Q671), E580 (≠ D672), R582 (≠ F674)
- binding iron/sulfur cluster: H99 (= H116), D102 (= D119), C103 (= C120), C106 (= C123), G109 (≠ N126), C112 (= C129), Q115 (= Q132), C152 (= C171), V153 (≠ I172), L154 (≠ V173), C155 (= C174), A156 (≠ N175), R157 (= R176), C158 (= C177), C202 (= C224), P203 (= P225), V204 (≠ T226), A206 (≠ T228), L207 (= L229), C228 (= C248), C231 (= C251), S233 (≠ V253), C235 (= C255), N262 (≠ S282), C263 (= C283), G266 (= G286), P391 (= P418), I392 (≠ V419)
Sites not aligning to the query:
8a6tA Cryo-em structure of the electron bifurcating fe-fe hydrogenase hydabc complex from thermoanaerobacter kivui in the reduced state (see paper)
42% identity, 22% coverage: 24:236/962 of query aligns to 4:211/571 of 8a6tA
- binding fe2/s2 (inorganic) cluster: C36 (= C56), D37 (≠ A57), C47 (= C67), R48 (= R68), C50 (= C70), C63 (= C84)
- binding iron/sulfur cluster: H95 (= H116), C99 (= C120), C102 (= C123), C108 (= C129), C146 (= C171), C149 (= C174), G150 (≠ N175), K151 (≠ R176), C152 (= C177), C156 (= C181), C189 (= C214), C192 (= C217), C195 (= C220), C199 (= C224), G202 (≠ A227)
Sites not aligning to the query:
- binding 2 iron/2 sulfur/5 carbonyl/2 water inorganic cluster: 229, 230, 231, 298, 323, 352, 353, 357, 412, 500
- binding iron/sulfur cluster: 299, 354, 496, 500
8a5eA Cryo-em structure of the electron bifurcating fe-fe hydrogenase hydabc complex from acetobacterium woodii in the reduced state (see paper)
40% identity, 24% coverage: 23:249/962 of query aligns to 3:231/583 of 8a5eA
- binding fe2/s2 (inorganic) cluster: T34 (≠ K54), C36 (= C56), G45 (= G65), C47 (= C67), C50 (= C70), C64 (= C84)
- binding iron/sulfur cluster: H96 (= H116), N97 (≠ P117), C100 (= C120), C103 (= C123), S106 (≠ N126), C109 (= C129), C148 (= C171), C151 (= C174), K152 (≠ N175), C154 (= C177), C158 (= C181), V166 (≠ A189), C191 (= C214), C194 (= C217), G195 (= G218), C197 (= C220), C201 (= C224), P202 (= P225), V203 (≠ T226)
Sites not aligning to the query:
7b0nG 3.7-angstrom structure of Yarrowia lipolytica complex I with an R121M mutation in NUCM. (see paper)
28% identity, 51% coverage: 23:513/962 of query aligns to 2:480/694 of 7b0nG
- binding fe2/s2 (inorganic) cluster: C35 (= C56), G44 (= G65), C46 (= C67), R47 (= R68), C49 (= C70), C63 (= C84)
- binding iron/sulfur cluster: H95 (= H116), C99 (= C120), C102 (= C123), C108 (= C129), Q111 (= Q132), C149 (= C171), H151 (≠ V173), C152 (= C174), T153 (≠ N175), C155 (= C177), C199 (= C224), V201 (≠ T226)
P39185 Periplasmic nitrate reductase; EC 1.9.6.1 from Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) (Ralstonia eutropha) (see 2 papers)
26% identity, 49% coverage: 248:716/962 of query aligns to 48:556/831 of P39185
- C48 (= C248) binding
- C51 (= C251) binding
- C55 (= C255) binding
- C83 (= C283) binding
- K85 (= K285) binding
- Q152 (≠ R347) binding
- N177 (≠ C372) binding
- C181 (= C376) binding
- 214:221 (vs. 409:416, 25% identical) binding
- STFTH 245:249 (≠ DP--- 438:439) binding
- QTD 264:266 (≠ GTN 461:463) binding
- M375 (≠ L541) binding
- Q379 (≠ E545) binding
- N485 (≠ D647) binding
- SD 511:512 (≠ QD 671:672) binding
- K534 (= K694) binding
Sites not aligning to the query:
- 1:29 signal peptide, Tat-type signal
- 561 binding
- 721:730 binding
- 805 binding
- 822 binding
Query Sequence
>AO353_15690 AO353_15690 formate dehydrogenase
MITLFDPNTDIDLGTPARHSEVQITLNIDGQSISVPEGTSVMRAAAMLGTTIPKLCATDS
LEAFGSCRMCLVEIDGMRGYPASCTTPVSEGMSVHTQTPKLATLRRNVMELYISDHPLDC
LTCSANGNCELQTVAGQVGLREVRYGYEGENHLDDQKDTSNPYFDYDPSKCIVCNRCVRA
CEETQGTFALTITGRGFESRVAAAGGENFLDSECVSCGACVQACPTATLMEKSVVELGQP
EHSVITTCAYCGVGCSFRAEMKGDQVVRMVPDKNGQANHGHSCVKGRFAWGYATHPDRIT
KPMIRKHINDPWQEVSWDEAVTYAASEFRRLQQKYGRDSIGGITSSRCTNEETYLVQKLV
RAAFGNNNVDTCARVCHSPTGYGLKQTLGESAGTQSFDSVMQADVILVMGANPSDAHPVF
ASQLKRRLREGARLIVIDPRRIDLVDTVHARAELHLALRPGTNVAMLNALAHVIVTEGLL
NQAFIDARCEGSDFAQWKAFVSRAENSPEVLGEICGVAAADIRAAARLYATGGNAAIYYG
LGVTEHSQGSTAVMGIANLAMVTGNIGREGVGVNPLRGQNNVQGSCDMGSFPHELPGYRH
ISNEVVRAQFEQAWNVTLQPDPGLRIPNMFEAALGGSFKGLYCQGEDIAQSDPNTQHVTA
ALSAMECIVVQDIFLNETAKFAHVFLPGSSFLEKDGTFTNAERRISRVRKVMEPLGGKAD
WEGTVALANALGYPMNYQHPSEIMDEIASLTPTFTNVSYASLDRHGSLQWPCNAAAPDGT
PTMHIEEFVRGKGRFMLTGYVPTEEKVNSRYPLLLTTGRILSQYNVGAQTRRTENVAWHD
EDRLEIHPTDAESRGINEGDWVGIGSRAGQTVLRARITERVAPGVVYTTFHFPESGANVI
TTDNSDWATNCPEYKVTAVEVSRVYHPSEWQKRYQEFSDEQQRLLDERRQARAAGAKAEV
RR
Or try a new SitesBLAST search
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