SitesBLAST

O52681 Bifurcating [FeFe] hydrogenase gamma subunit; Hydrogenase (NAD(+), ferredoxin) gamma subunit; Iron-hydrogenase gamma subunit; EC 1.12.1.4 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
29% identity, 84% coverage: 26:157/158 of query aligns to 22:153/161 of O52681

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O52681

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D79 (≠ R83) mutation to P: Increase (30 mV) in the redox potential.
G80 (≠ A84) mutation to P: Large decrease (149 mV) in the redox potential. Causes a change to a [4Fe-4S] cluster protein.
T81 (≠ E85) mutation to P: Small increase (11 mV) in the redox potential.
A82 (= A86) mutation to P: Decrease (46 mV) in the redox potential.
L120 (= L124) mutation to P: Large decrease (65 mV) in the redox potential.
G121 (= G125) mutation to P: Decrease (22 mV) in the redox potential.
A122 (≠ Q126) mutation to P: Large decrease (132 mV) in the redox potential.
V128 (≠ N132) mutation V->A,C,H,Y: Small increase (about 2-14 mV) in the redox potential.; mutation V->D,G,R,S,T,W: Increase (about 23-33 mV) in the redox potential.; mutation V->E,K,L,M: Decrease (about 37-50 mV) in the redox potential.; mutation V->F,I,P,Q: Small decrease (about 4-20 mV) in the redox potential.; mutation to N: Large increase (85 mV) in the redox potential.

7p5hC Tmhydabc- d2 map (see paper)
29% identity, 84% coverage: 26:157/158 of query aligns to 19:150/156 of 7p5hC

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7p5hC

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binding fe2/s2 (inorganic) cluster: C75 (= C82), G77 (≠ A84), A79 (= A86), C80 (= C87), C116 (= C123), L117 (= L124), A119 (≠ Q126), C120 (= C127)

8e9gE Mycobacterial respiratory complex i with both quinone positions modelled (see paper)
31% identity, 91% coverage: 15:157/158 of query aligns to 35:177/233 of 8e9gE

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binding fe2/s2 (inorganic) cluster: C102 (= C82), C107 (= C87), C143 (= C123), N144 (≠ L124), A145 (≠ G125), A146 (≠ Q126), C147 (= C127), V152 (≠ N132)

5gupE structure of mammalian respiratory supercomplex I1III2IV1 (see paper)
31% identity, 82% coverage: 23:152/158 of query aligns to 54:183/197 of 5gupE

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5gupE

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binding fe2/s2 (inorganic) cluster: C113 (= C82), T115 (≠ A84), P117 (≠ A86), C118 (= C87), C154 (= C123), L155 (= L124), G156 (= G125), A157 (≠ Q126), C158 (= C127), M163 (≠ N132)

P19404 NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial; NDUFV2; NADH-ubiquinone oxidoreductase 24 kDa subunit; EC 7.1.1.2 from Homo sapiens (Human) (see 2 papers)
32% identity, 82% coverage: 23:152/158 of query aligns to 76:205/249 of P19404

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P19404

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Y193 (≠ H140) modified: Phosphotyrosine; by SRC

Sites not aligning to the query:

29 V → A: in dbSNP:rs906807

Q56221 NADH-quinone oxidoreductase subunit 2; NADH dehydrogenase I chain 2; NDH-1 subunit 2; EC 7.1.1.- from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see 2 papers)
33% identity, 72% coverage: 25:138/158 of query aligns to 26:139/181 of Q56221

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Q56221

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C83 (= C82) binding
S87 (≠ A86) binding
C88 (= C87) binding
C124 (= C123) binding
C128 (= C127) binding

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
144 modified: Disulfide link with 172
172 modified: Disulfide link with 144

3i9v2 Crystal structure of the hydrophilic domain of respiratory complex i from thermus thermophilus, oxidized, 2 mol/asu (see paper)
33% identity, 72% coverage: 25:138/158 of query aligns to 24:137/178 of 3i9v2

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3i9v2

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binding fe2/s2 (inorganic) cluster: C81 (= C82), T83 (≠ A84), S85 (≠ A86), C86 (= C87), C122 (= C123), L123 (= L124), G124 (= G125), S125 (≠ Q126), C126 (= C127)
binding manganese (ii) ion: S66 (≠ H67), V120 (= V121), E121 (≠ Y122)

3iam2 Crystal structure of the hydrophilic domain of respiratory complex i from thermus thermophilus, reduced, 2 mol/asu, with bound nadh (see paper)
33% identity, 72% coverage: 25:138/158 of query aligns to 25:138/179 of 3iam2

query
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3iam2

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binding fe2/s2 (inorganic) cluster: C82 (= C82), C87 (= C87), C123 (= C123), C127 (= C127)

7dgq9 NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial (see paper)
31% identity, 82% coverage: 23:152/158 of query aligns to 37:166/207 of 7dgq9

query
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7dgq9

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D

A

S

L

I

A

L

E

E

H

A

A

I

Q

Q

N

K

V

K

L

L

G

G

C

I

G

K

F

V

H

G

D

E

T

T

S

T

A

P

D

D

G

K

Q

L

F

F

T

T

L

L

E

I

P

E

V

V

Y

E

C
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C

L
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L

G

G

Q
x
A

C
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C

A

V

I

N

G

A

P

P

N

M

L

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T

Q

L

I

D

N

D

D

E

N

L

Y

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Y

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D

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D

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A

P

D

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K

D

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I

binding fe2/s2 (inorganic) cluster: C96 (= C82), T98 (≠ A84), C101 (= C87), C137 (= C123), L138 (= L124), A140 (≠ Q126), C141 (= C127)
binding : R49 (≠ E35)

Sites not aligning to the query:

binding : 20, 23, 29, 32, 35

P04394 NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial; NADH dehydrogenase subunit II; NADH-ubiquinone oxidoreductase 24 kDa subunit; EC 7.1.1.2 from Bos taurus (Bovine) (see 2 papers)
31% identity, 82% coverage: 23:152/158 of query aligns to 76:205/249 of P04394

query
sites
P04394

A

A

G

A

A

A

M

V

L

L

P

P

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L

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D

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A

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C
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C

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C

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M

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G

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G

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E

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A

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L

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A

L

E

E

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A

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Q

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L

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F

F

T

T

L

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Y

E

C
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C

L

L

G

G

Q

A

C
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C

A

V

I

N

G

A

P

P

N

M

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T

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L

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D

N

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I

C135 (= C82) binding
C140 (= C87) binding
C176 (= C123) binding
C180 (= C127) binding

Sites not aligning to the query:

1:32 modified: transit peptide, Mitochondrion

7v2cO Active state complex i from q10 dataset (see paper)
31% identity, 82% coverage: 23:152/158 of query aligns to 44:173/217 of 7v2cO

query
sites
7v2cO

A

A

G

A

A

A

M

V

L

L

P

P

I

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L

L

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D

G

L

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A

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A

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F

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F

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P

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C

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T

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T

A
x
P

C
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C

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M

A

L

R

R

G

N

G

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E

D

A

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L

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A

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E

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H

A

A

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Q

N

K

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L

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C

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T

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F

T

T

L

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E

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P

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Y

E

C
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C

L
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L

G
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G

Q
x
A

C
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C

A

V

I

N

G

A

P

P

N

M

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Q

L

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N

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N

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binding fe2/s2 (inorganic) cluster: C103 (= C82), P107 (≠ A86), C108 (= C87), C144 (= C123), L145 (= L124), G146 (= G125), A147 (≠ Q126), C148 (= C127)

Query Sequence

>HSERO_RS07420 FitnessBrowser__HerbieS:HSERO_RS07420
MKRQQVFDVAAVRGIIAERKEMAGAMLPILHGIQEKVGYIPADAVPMIAGELNVSRAEVH
GVISFYHFFRQEPAGRHVVQVCRAEACQARGGEALAEHAQNVLGCGFHDTSADGQFTLEP
VYCLGQCAIGPNLTLDDELHARVDADKFKRLIQAKREA

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