SitesBLAST
Comparing WP_012103136.1 NCBI__GCF_000016505.1:WP_012103136.1 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 20 (the maximum) hits to proteins with known functional sites (download)
4om8A Crystal structure of 5-formly-3-hydroxy-2-methylpyridine 4-carboxylic acid (fhmpc) 5-dehydrogenase, an NAD+ dependent dismutase. (see paper)
34% identity, 94% coverage: 3:303/319 of query aligns to 2:299/309 of 4om8A
- active site: S116 (= S120), H137 (= H141), E149 (= E153), N188 (= N192)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), T12 (= T13), M13 (= M14), Y31 (≠ F32), D32 (≠ G33), V33 (≠ R34), N86 (≠ C90), V87 (≠ I91), P88 (≠ A92), E89 (= E93), K94 (= K98), D114 (≠ N118), H137 (= H141)
Q988C8 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylate 5-dehydrogenase; FHMPC dehydrogenase; EC 1.2.1.100 from Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) (Mesorhizobium loti (strain MAFF 303099)) (see 2 papers)
34% identity, 94% coverage: 3:303/319 of query aligns to 2:299/309 of Q988C8
- TM 12:13 (= TM 13:14) binding NAD(+)
- D32 (≠ G33) binding NAD(+)
- VPE 87:89 (≠ IAE 91:93) binding NAD(+)
- K94 (= K98) binding NAD(+)
- H137 (= H141) mutation to L: Loss of activity.
- E149 (= E153) mutation to Q: Shows a different pH optimum depending on the cosubstrate.
4kugA Crystal structure of 3-hydroxybutylryl-coa dehydrogenase with NAD from clostridium butyricum
40% identity, 89% coverage: 3:287/319 of query aligns to 1:281/282 of 4kugA
- active site: S117 (= S120), H138 (= H141), E150 (= E153), N188 (= N192)
- binding nicotinamide-adenine-dinucleotide: G10 (= G12), T11 (= T13), M12 (= M14), R30 (≠ F32), D31 (≠ G33), A87 (≠ C90), A88 (≠ I91), E90 (= E93), N115 (= N118), S117 (= S120), H138 (= H141)
4kuhA Crystal structure of 3-hydroxybutylryl-coa dehydrogenase with acetoacetyl-coa from clostridium butyricum
40% identity, 89% coverage: 3:286/319 of query aligns to 1:280/280 of 4kuhA
6aa8E Crystal structure of (s)-3-hydroxybutyryl-coenzymea dehydrogenase from clostridium acetobutylicum complexed with NAD+ (see paper)
40% identity, 89% coverage: 4:287/319 of query aligns to 1:280/281 of 6aa8E
- active site: S116 (= S120), H137 (= H141), E149 (= E153), N187 (= N192)
- binding nicotinamide-adenine-dinucleotide: I6 (≠ L9), G9 (= G12), T10 (= T13), M11 (= M14), R29 (≠ F32), D30 (≠ G33), I31 (≠ R34), A86 (≠ C90), A87 (≠ I91), E89 (= E93), K94 (= K98), N114 (= N118), S116 (= S120)
4pzeA Crystal structure of (s)-3-hydroxybutyryl-coa dehydrogenase paah1 in complex with acetoacetyl-coa (see paper)
34% identity, 89% coverage: 3:287/319 of query aligns to 2:282/283 of 4pzeA
4pzdA Crystal structure of (s)-3-hydroxybutyryl-coa dehydrogenase paah1 in complex with NAD+ (see paper)
34% identity, 89% coverage: 3:287/319 of query aligns to 2:282/283 of 4pzdA
- active site: S118 (= S120), H139 (= H141), E151 (= E153), N189 (= N192)
- binding nicotinamide-adenine-dinucleotide: G11 (= G12), T12 (= T13), M13 (= M14), D32 (≠ G33), A88 (≠ C90), A89 (≠ I91), T90 (≠ A92), E91 (= E93), I99 (≠ V101), N116 (= N118), S118 (= S120), N142 (= N144)
Q9Y2S2 Lambda-crystallin homolog; L-gulonate 3-dehydrogenase; Gul3DH; EC 1.1.1.45 from Homo sapiens (Human)
35% identity, 77% coverage: 6:251/319 of query aligns to 9:255/319 of Q9Y2S2
- VI 16:17 (≠ TM 13:14) binding NAD(+)
- D36 (≠ G33) binding NAD(+)
- E97 (= E93) binding NAD(+)
- K102 (= K98) binding NAD(+)
3f3sA The crystal structure of human lambda-crystallin, cryl1
35% identity, 77% coverage: 6:251/319 of query aligns to 5:251/312 of 3f3sA
- active site: S120 (= S120), H141 (= H141), E153 (= E153), N192 (= N192)
- binding nicotinamide-adenine-dinucleotide: G9 (= G10), G11 (= G12), V12 (≠ T13), I13 (≠ M14), D32 (≠ G33), I33 (≠ R34), C90 (= C90), V91 (≠ I91), P92 (≠ A92), E93 (= E93), L97 (= L97), K98 (= K98), I101 (≠ V101), S118 (≠ N118), H141 (= H141), N144 (= N144), N240 (≠ G240), Y251 (= Y251)
P9WNP7 3-hydroxybutyryl-CoA dehydrogenase; Beta-hydroxybutyryl-CoA dehydrogenase; BHBD; EC 1.1.1.157 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
34% identity, 89% coverage: 3:286/319 of query aligns to 5:286/286 of P9WNP7
- S122 (= S120) mutation to A: Loss of fatty acyl dehydrogenase activity.
D7URM0 L-carnitine dehydrogenase; CDH; L-CDH; EC 1.1.1.108 from Pseudomonas sp. (see paper)
35% identity, 76% coverage: 3:243/319 of query aligns to 7:243/321 of D7URM0
Sites not aligning to the query:
- 317:321 mutation Missing: Marked decrease in catalytic activity.
1f0yA L-3-hydroxyacyl-coa dehydrogenase complexed with acetoacetyl-coa and NAD+ (see paper)
35% identity, 89% coverage: 3:286/319 of query aligns to 4:290/291 of 1f0yA
- active site: S126 (= S120), H147 (= H141), E159 (= E153), N197 (= N192)
- binding acetoacetyl-coenzyme a: S50 (= S49), K57 (= K51), S126 (= S120), H147 (= H141), F149 (≠ W143), N150 (= N144), P151 (= P145), P153 (≠ Q147), V154 (≠ F148), N197 (= N192), P232 (≠ R227), M233 (≠ L228), L238 (≠ S236)
- binding nicotinamide-adenine-dinucleotide: G13 (= G12), L14 (≠ T13), M15 (= M14), D34 (≠ G33), Q35 (≠ R34), A96 (≠ C90), I97 (= I91), E99 (= E93), K104 (= K98), N124 (= N118), S126 (= S120), H147 (= H141), N150 (= N144), V242 (≠ G240), T246 (≠ I244), K282 (= K278)
Q16836 Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial; HCDH; Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase; Short-chain 3-hydroxyacyl-CoA dehydrogenase; EC 1.1.1.35 from Homo sapiens (Human) (see 7 papers)
35% identity, 89% coverage: 3:286/319 of query aligns to 27:313/314 of Q16836
- GGGLMG 34:39 (≠ GTGTMG 10:15) binding NAD(+)
- A40 (≠ N16) to T: in HADH deficiency; dbSNP:rs137853101
- D57 (≠ G33) binding NAD(+); to E: in HADH deficiency; dbSNP:rs137853102; to G: found in a patient with Reye-like syndrome; does not affect 3-hydroxyacyl-CoA dehydrogenase activity; increases KM value for NADH; does not affect dimerization
- S73 (= S49) binding CoA
- K80 (= K56) binding CoA
- L86 (≠ I63) to P: in dbSNP:rs4956145
- E122 (= E93) binding NAD(+)
- K127 (= K98) binding NAD(+); modified: N6-(2-hydroxyisobutyryl)lysine
- S149 (= S120) binding CoA; binding NAD(+)
- Q152 (≠ S123) to H: in dbSNP:rs1051519
- N173 (= N144) binding NAD(+)
- Y226 (≠ L198) to H: found in a patient with Reye-like syndrome; loss of 3-hydroxyacyl-CoA dehydrogenase activity. Does not affect dimerization; dbSNP:rs146036912
- P258 (= P233) to L: in HHF4; loss of 3-hydroxyacyl-CoA dehydrogenase activity; dbSNP:rs137853103
- K305 (= K278) binding NAD(+)
P00348 Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial; HCDH; L-3-hydroxyacyl CoA dehydrogenase; Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase; Short-chain 3-hydroxyacyl-CoA dehydrogenase; EC 1.1.1.35 from Sus scrofa (Pig) (see paper)
34% identity, 89% coverage: 3:286/319 of query aligns to 27:313/314 of P00348
- GGGLMG 34:39 (≠ GTGTMG 10:15) binding NAD(+)
- D57 (≠ G33) binding NAD(+)
- E122 (= E93) binding NAD(+)
- K127 (= K98) binding NAD(+)
- S149 (= S120) binding NAD(+)
1f17A L-3-hydroxyacyl-coa dehydrogenase complexed with nadh (see paper)
35% identity, 90% coverage: 3:289/319 of query aligns to 4:293/293 of 1f17A
- active site: S126 (= S120), H147 (= H141), E159 (= E153), N197 (= N192)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G13 (= G12), L14 (≠ T13), M15 (= M14), D34 (≠ G33), Q35 (≠ R34), A96 (≠ C90), I97 (= I91), E99 (= E93), K104 (= K98), N124 (= N118), S126 (= S120), H147 (= H141)
1f12A L-3-hydroxyacyl-coa dehydrogenase complexed with 3-hydroxybutyryl-coa (see paper)
35% identity, 90% coverage: 3:289/319 of query aligns to 4:293/293 of 1f12A
- active site: S126 (= S120), H147 (= H141), E159 (= E153), N197 (= N192)
- binding 3-hydroxybutanoyl-coenzyme a: K57 (= K51), S126 (= S120), H147 (= H141), F149 (≠ W143), N150 (= N144), M155 (≠ I149), N197 (= N192), L200 (≠ Q195), P232 (≠ R227), M233 (≠ L228), L238 (≠ S236)
3adpA Crystal structure of the rabbit l-gulonate 3-dehydrogenase (nadh form)
33% identity, 77% coverage: 5:251/319 of query aligns to 2:249/310 of 3adpA
- active site: S118 (= S120), H139 (= H141), E151 (= E153), N190 (= N192)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G9 (= G12), L10 (≠ T13), V11 (≠ M14), D30 (≠ G33), I31 (≠ R34), Q35 (≠ S38), C88 (= C90), V89 (≠ I91), P90 (≠ A92), E91 (= E93), K96 (= K98), I99 (≠ V101), S116 (≠ N118), S118 (= S120), H139 (= H141), P140 (≠ F142), N142 (= N144)
P14755 Lambda-crystallin; L-gulonate 3-dehydrogenase; Gul3DH; EC 1.1.1.45 from Oryctolagus cuniculus (Rabbit) (see paper)
33% identity, 77% coverage: 5:251/319 of query aligns to 8:255/319 of P14755
- LV 16:17 (≠ TM 13:14) binding NAD(+)
- D36 (≠ G33) binding NAD(+); mutation to R: Reduces enzyme activity and alters specificity, so that NADP can be used as cosubstrate.
- E97 (= E93) binding NAD(+)
- K102 (= K98) binding NAD(+)
- S124 (= S120) mutation to A: Reduces enzyme activity 500-fold.
- H145 (= H141) mutation to Q: Abolishes enzyme activity.
- E157 (= E153) mutation to Q: No major effect on enzyme activity.
- N196 (= N192) mutation N->D,Q: Abolishes enzyme activity.
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
33% identity, 99% coverage: 3:317/319 of query aligns to 291:594/692 of 6iunB
- active site: S407 (= S120), H428 (= H141), E440 (= E153), N478 (= N192)
- binding nicotinamide-adenine-dinucleotide: G300 (= G12), T301 (= T13), M302 (= M14), E321 (≠ G33), T322 (≠ R34), Y365 (≠ I77), A377 (≠ C90), V378 (≠ I91), E380 (= E93), V384 (≠ L97), V388 (= V101), N405 (= N118), S407 (= S120)
Sites not aligning to the query:
3zwaA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 3s-hydroxy-hexanoyl-coa (see paper)
30% identity, 89% coverage: 3:286/319 of query aligns to 302:587/727 of 3zwaA
Sites not aligning to the query:
- active site: 67, 72, 82, 106, 109, 128, 129, 136, 137, 255
- binding (S)-3-Hydroxyhexanoyl-CoA: 27, 65, 66, 67, 68, 69, 104, 109, 124, 129, 132, 137, 162
Query Sequence
>WP_012103136.1 NCBI__GCF_000016505.1:WP_012103136.1
MDIKNVAVLGTGTMGNGIVQLCAESGLNVNMFGRTDASLERGFTSIKTSLKNLEEKGKIK
TNISKEILKRIKGVKTIEEAVEGVDFVIECIAEDLELKQEVFSKLDEICAPEVILASNTS
GLSPTDIAINTKHPERVVIAHFWNPPQFIPLVEVVPGKHTDSKTVDITMDWIEHIGKKGV
KMRKECLGFIGNRLQLALLREALYIVEQGFATAEEVDKAIEYGHGRRLPVTGPICSADLG
GLDIFNNISSYLFKDLCNDTEPSKLLKSKVDGGNLGSKTGKGFYNWTPEFLQKKQNERIQ
LLMDFLEKDKNDKSIERNI
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