SitesBLAST
Comparing H281DRAFT_01850 FitnessBrowser__Burk376:H281DRAFT_01850 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)
5z20F The ternary structure of d-lactate dehydrogenase from pseudomonas aeruginosa with nadh and oxamate (see paper)
54% identity, 98% coverage: 1:323/331 of query aligns to 8:330/336 of 5z20F
- active site: S108 (= S101), R241 (= R234), D265 (= D258), E270 (= E263), H302 (= H295)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y107 (= Y100), G160 (= G153), Q161 (≠ K154), I162 (= I155), Y180 (= Y173), D181 (= D174), P182 (≠ K175), C212 (= C205), P213 (= P206), T218 (= T211), T239 (= T232), G240 (≠ S233), R241 (= R234), H302 (= H295), A304 (= A297)
4cukA Structure of salmonella d-lactate dehydrogenase in complex with nadh
51% identity, 99% coverage: 1:328/331 of query aligns to 1:328/330 of 4cukA
- active site: S101 (= S101), R234 (= R234), D258 (= D258), E263 (= E263), H295 (= H295)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y100 (= Y100), G153 (= G153), K154 (= K154), I155 (= I155), F173 (≠ Y173), D174 (= D174), P175 (≠ K175), H204 (= H204), C205 (= C205), P206 (= P206), N211 (≠ T211), T232 (= T232), Y260 (= Y260), H295 (= H295), A297 (= A297)
8grvA Dictyostelium discoideum lactate dehydrogenase (dicldha)with NAD
42% identity, 100% coverage: 1:331/331 of query aligns to 3:329/336 of 8grvA
- binding nicotinamide-adenine-dinucleotide: V106 (= V105), G154 (= G153), N155 (≠ K154), I156 (= I155), D176 (= D174), I177 (≠ K175), I178 (≠ F176), T208 (≠ C205), P209 (= P206), T214 (= T211), V235 (≠ T232), H298 (= H295), A300 (= A297), W301 (≠ F298)
4zgsA Identification of the pyruvate reductase of chlamydomonas reinhardtii (see paper)
44% identity, 98% coverage: 6:330/331 of query aligns to 16:346/346 of 4zgsA
- active site: S111 (= S101), R244 (= R234), D268 (= D258), E273 (= E263), H311 (= H295)
- binding nicotinamide-adenine-dinucleotide: Y110 (= Y100), G163 (= G153), A164 (≠ K154), I165 (= I155), D184 (= D174), C215 (= C205), P216 (= P206), L218 (≠ T208), S220 (≠ E210), T221 (= T211), S243 (= S233), H311 (= H295), F314 (= F298)
5z21B The ternary structure of d-lactate dehydrogenase from fusobacterium nucleatum with nadh and oxamate (see paper)
45% identity, 98% coverage: 3:328/331 of query aligns to 4:329/331 of 5z21B
- active site: S101 (= S101), R235 (= R234), D259 (= D258), E264 (= E263), H296 (= H295)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y100 (= Y100), I105 (≠ V105), G153 (= G153), K154 (= K154), I155 (= I155), D174 (= D174), L175 (≠ K175), P207 (= P206), T212 (= T211), T233 (= T232), G234 (≠ S233), R235 (= R234), H296 (= H295), Y299 (≠ F298)
P26297 D-lactate dehydrogenase; D-LDH; D-specific 2-hydroxyacid dehydrogenase; EC 1.1.1.28 from Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM 00102 / Lb 14) (see 2 papers)
37% identity, 95% coverage: 9:322/331 of query aligns to 14:324/333 of P26297
- HI 156:157 (≠ KI 154:155) binding
- D176 (= D174) binding
- H206 (= H204) mutation to Q: Increase of activity.
- VP 207:208 (≠ CP 205:206) binding
- N213 (≠ T211) binding
- R236 (= R234) mutation to K: Decrease of activity.
- D260 (= D258) binding ; mutation to N: Decrease of activity.
- E265 (= E263) mutation to Q: Decrease of activity.
- H297 (= H295) mutation to Q: 90% loss of activity.
1j49A Insights into domain closure, substrate specificity and catalysis of d-lactate dehydrogenase from lactobacillus bulgaricus (see paper)
37% identity, 95% coverage: 9:322/331 of query aligns to 14:324/332 of 1j49A
- active site: S103 (= S101), R236 (= R234), D260 (= D258), E265 (= E263), H297 (= H295)
- binding nicotinamide-adenine-dinucleotide: Y102 (= Y100), I107 (≠ V105), G153 (= G151), G155 (= G153), I157 (= I155), Y175 (= Y173), D176 (= D174), I177 (≠ K175), V207 (≠ C205), P208 (= P206), N213 (≠ T211), V234 (≠ T232), S235 (= S233), R236 (= R234), H297 (= H295), A299 (= A297), F300 (= F298)
2dldA D-lactate dehydrogenase complexed with nadh and oxamate
36% identity, 92% coverage: 6:308/331 of query aligns to 7:310/337 of 2dldA
- active site: S103 (= S101), R236 (= R234), D260 (= D258), E265 (= E263), H297 (= H295)
- binding 1,4-dihydronicotinamide adenine dinucleotide: T154 (= T152), G155 (= G153), H156 (≠ K154), I157 (= I155), D176 (= D174), I177 (≠ K175), V207 (≠ C205), P208 (= P206), N213 (≠ T211), C234 (≠ T232), S235 (= S233), H297 (= H295)
Sites not aligning to the query:
P30901 D-lactate dehydrogenase; D-LDH; D-specific 2-hydroxyacid dehydrogenase; EC 1.1.1.28 from Lactobacillus helveticus (Lactobacillus suntoryeus) (see paper)
36% identity, 92% coverage: 6:308/331 of query aligns to 7:310/337 of P30901
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3kb6B Crystal structure of d-lactate dehydrogenase from aquifex aeolicus complexed with NAD and lactic acid (see paper)
34% identity, 83% coverage: 48:321/331 of query aligns to 46:320/334 of 3kb6B
- active site: S97 (= S101), R231 (= R234), D255 (= D258), E260 (= E263), H294 (= H295)
- binding lactic acid: F49 (= F51), S72 (≠ C76), V73 (≠ T77), G74 (= G78), Y96 (= Y100), R231 (= R234), H294 (= H295)
- binding nicotinamide-adenine-dinucleotide: V73 (≠ T77), Y96 (= Y100), V101 (= V105), G150 (= G153), R151 (≠ K154), I152 (= I155), D171 (= D174), V172 (≠ K175), P203 (= P206), T229 (= T232), A230 (≠ S233), R231 (= R234), H294 (= H295), A296 (= A297), Y297 (≠ F298)
1dxyA Structure of d-2-hydroxyisocaproate dehydrogenase (see paper)
30% identity, 100% coverage: 1:330/331 of query aligns to 1:330/330 of 1dxyA
- active site: S101 (= S101), R234 (= R234), D258 (= D258), E263 (= E263), H295 (= H295)
- binding 2-oxo-4-methylpentanoic acid: V77 (≠ T77), Y100 (= Y100), Y298 (≠ F298)
- binding nicotinamide-adenine-dinucleotide: Y100 (= Y100), G152 (= G151), G154 (= G153), H155 (≠ K154), I156 (= I155), Y174 (= Y173), D175 (= D174), P176 (≠ K175), H204 (= H204), V205 (≠ C205), P206 (= P206), N211 (≠ T211), T232 (= T232), A233 (≠ S233), R234 (= R234), H295 (= H295), Y298 (≠ F298)
P17584 D-2-hydroxyisocaproate dehydrogenase; D-HICDH; EC 1.1.1.- from Lacticaseibacillus paracasei (Lactobacillus paracasei) (see paper)
30% identity, 100% coverage: 1:330/331 of query aligns to 1:330/333 of P17584
4prlA Crystal structure of d-lactate dehydrogenase with NAD+ from lactobacillus jensenii (see paper)
33% identity, 97% coverage: 1:322/331 of query aligns to 1:322/330 of 4prlA
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y100), I106 (≠ V105), V154 (≠ T152), G155 (= G153), H156 (≠ K154), I157 (= I155), Y175 (= Y173), D176 (= D174), H205 (= H204), T206 (≠ C205), P207 (= P206), A233 (≠ T232), A234 (≠ S233), D259 (= D258), H295 (= H295), A297 (= A297)
4xkjA A novel d-lactate dehydrogenase from sporolactobacillus sp
32% identity, 95% coverage: 1:315/331 of query aligns to 1:315/332 of 4xkjA
- active site: S102 (= S101), R234 (= R234), D258 (= D258), E263 (= E263), H295 (= H295)
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y100), V106 (= V105), G152 (= G151), G154 (= G153), R155 (≠ K154), I156 (= I155), D175 (= D174), I176 (≠ K175), R179 (≠ S178), H204 (= H204), V205 (≠ C205), P206 (= P206), T211 (= T211), A232 (≠ T232), R234 (= R234), H295 (= H295), G297 (≠ A297), F298 (= F298)
2yq5C Crystal structure of d-isomer specific 2-hydroxyacid dehydrogenase from lactobacillus delbrueckii ssp. Bulgaricus: NAD complexed form (see paper)
31% identity, 98% coverage: 3:325/331 of query aligns to 3:328/331 of 2yq5C
- active site: S102 (= S101), R236 (= R234), D260 (= D258), E265 (= E263), H297 (= H295)
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y100), I106 (≠ V105), V155 (≠ T152), G156 (= G153), H157 (≠ K154), I158 (= I155), Y176 (= Y173), D177 (= D174), V178 (≠ K175), H206 (= H204), T207 (≠ C205), P208 (= P206), A235 (≠ S233), R236 (= R234), H297 (= H295), F300 (= F298)
O43175 D-3-phosphoglycerate dehydrogenase; 3-PGDH; 2-oxoglutarate reductase; Malate dehydrogenase; EC 1.1.1.95; EC 1.1.1.399; EC 1.1.1.37 from Homo sapiens (Human) (see 3 papers)
33% identity, 77% coverage: 77:330/331 of query aligns to 78:318/533 of O43175
- T78 (= T77) binding
- R135 (≠ L134) to W: in PHGDHD; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity; dbSNP:rs267606949
- RI 155:156 (≠ KI 154:155) binding
- D175 (= D174) binding
- T207 (≠ C205) binding
- CAR 234:236 (≠ TSR 232:234) binding
- D260 (= D258) binding
- V261 (= V259) to M: in PHGDHD; results in a four-fold decrease in substrate affinity and a slight increase in maximal enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs267606947
- HLGA 283:286 (≠ HQAF 295:298) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 373 A → T: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs201553627
- 377 G → S: in PHGDHD; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity; dbSNP:rs267606948
- 425 V → M: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs121907988
- 490 V → M: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs121907987
6rj3A Crystal structure of phgdh in complex with compound 15 (see paper)
35% identity, 69% coverage: 77:303/331 of query aligns to 72:285/297 of 6rj3A
6rj2A Crystal structure of phgdh in complex with compound 40 (see paper)
35% identity, 69% coverage: 77:303/331 of query aligns to 70:283/299 of 6rj2A
- binding ~{N}-[(1~{R})-1-[4-(ethanoylsulfamoyl)phenyl]ethyl]-2-methyl-5-phenyl-pyrazole-3-carboxamide: G146 (= G153), I148 (= I155), Y166 (= Y173), D167 (= D174), P168 (≠ K175), I169 (≠ F176), I170 (≠ P177), H198 (= H204), T199 (≠ C205), L208 (≠ I214), R228 (= R234)
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
35% identity, 69% coverage: 77:303/331 of query aligns to 72:285/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (≠ S101), A100 (≠ V105), R149 (≠ K154), I150 (= I155), Y168 (= Y173), D169 (= D174), P170 (≠ K175), I171 (≠ F176), H200 (= H204), T201 (≠ C205), P202 (= P206), T207 (= T211), C228 (≠ T232), A229 (≠ S233), R230 (= R234), H277 (= H295), G279 (≠ A297)
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
35% identity, 69% coverage: 77:303/331 of query aligns to 73:286/301 of 6rj5A
Query Sequence
>H281DRAFT_01850 FitnessBrowser__Burk376:H281DRAFT_01850
MDIAVFSAKPYDREYLNAANAGHHHRLQYFDVPLDIETVSLAANHGAVCIFVNDHADAAV
LQALVHGGTKLVALRCTGFNNVDLKAAQDLGIKVVRVVNYSPNAVAEHAVALLMAINRKI
QRAYNRTRDFNFSLDGLMGFDLNGKVVAVIGTGKIGRVFTKIMLGFGCSVIGYDKFPSAE
FEALGARYARPKEIGESADIISLHCPLTPETYHIIDASTLARAKRGALLINTSRGALIDT
EAVIDALKSGQLGGLAIDVYEQEADLFFRDLSGTIITDDVLQRLVTFPNVIVTGHQAFLT
REAVTTICETTLQSVTEFETGKPLSNEISAS
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