| Accession |
MF_01252 |
| Dates |
24-AUG-2004 (Created) 19-AUG-2008 (Last updated, Version 18) |
| Protein name |
| RecName: |
Full=Flavohemoprotein; |
| AltName: |
Full=Hemoglobin-like protein; |
| AltName: |
Full=Flavohemoglobin; |
| AltName: |
Full=Nitric oxide dioxygenase; Short=NO oxygenase; Short=NOD; EC=1.14.12.17; |
|
case <OC:Proteobacteria> or <OC:Bacillales>
FUNCTION: Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress (By similarity).
end case
CATALYTIC ACTIVITY: 2 NO + 2 O(2) + NAD(P)H = 2 NO(3)(-) + NAD(P)(+).
COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per subunit (By similarity).
COFACTOR: Binds 1 FAD per subunit (By similarity).
DOMAIN: Consists of two distinct domains; an N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H.
SIMILARITY: Belongs to the globin family. Two-domain flavohemoproteins subfamily.
SIMILARITY: In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
case <OC:Proteobacteria> or <OC:Bacillales>
end case
GO:0005344; Molecular function: oxygen transporter activity.
GO:0008941; Molecular function: nitric oxide dioxygenase activity.
GO:0015671; Biological process: oxygen transport.
| From: HMP_ECOLI (P24232) |
| Key |
|
From |
|
To |
|
Description |
|
Condition |
|
FTGroup |
| DOMAIN |
|
151 |
|
251 |
|
FAD-binding |
|
|
|
|
| NP_BIND |
|
204 |
|
207 |
|
FAD (By similarity) |
|
R-[QN]-Y-S |
|
|
| NP_BIND |
|
268 |
|
273 |
|
NADP (By similarity) |
|
G-[VI]-G-[QILAV]-T-P |
|
|
| NP_BIND |
|
389 |
|
392 |
|
FAD (By similarity) |
|
[CLFVT]-F-G-[PST] |
|
|
| REGION |
|
147 |
|
Cter |
|
Reductase |
|
|
|
|
| REGION |
|
259 |
|
Cter |
|
NAD or NADP-binding |
|
|
|
|
| ACT_SITE |
|
95 |
|
95 |
|
Charge relay system (By similarity) |
|
Y |
|
|
| ACT_SITE |
|
135 |
|
135 |
|
Charge relay system (By similarity) |
|
E |
|
|
| METAL |
|
85 |
|
85 |
|
Iron (heme proximal ligand) (By similarity) |
|
H |
|
|
| BINDING |
|
188 |
|
188 |
|
FAD (By similarity) |
|
Y |
|
|
| SITE |
|
29 |
|
29 |
|
Involved in heme-bound ligand stabilization and O-O bond activation (By similarity) |
|
Y |
|
|
| SITE |
|
84 |
|
84 |
|
Influences the redox potential of the prosthetic heme and FAD groups (By similarity) |
|
K |
|
|
| SITE |
|
388 |
|
388 |
|
Influences the redox potential of the prosthetic heme and FAD groups (By similarity) |
|
E |
|
|
| Size range: |
392-411 amino acids |
| Related UniRules: |
None |
| Template: |
P24232 (HMP_ECOLI); P39662 (HMP_RALEH); P26353 (HMP_SALTY): [Recover all] |
| Scope: |
Bacteria |
| Fusion: |
Nter: None; Cter: None |
| Duplicate: |
None |
| Plasmid encoded: |
in RALEU, RHIME |
View rule in raw text format (no links)