8A1V
Sodium pumping NADH-quinone oxidoreductase with substrate Q2
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006811 | biological_process | monoatomic ion transport |
A | 0006814 | biological_process | sodium ion transport |
A | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
B | 0005886 | cellular_component | plasma membrane |
B | 0006811 | biological_process | monoatomic ion transport |
B | 0006814 | biological_process | sodium ion transport |
B | 0010181 | molecular_function | FMN binding |
B | 0016020 | cellular_component | membrane |
B | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
B | 0022904 | biological_process | respiratory electron transport chain |
B | 0055085 | biological_process | transmembrane transport |
B | 1902444 | molecular_function | riboflavin binding |
C | 0005886 | cellular_component | plasma membrane |
C | 0006811 | biological_process | monoatomic ion transport |
C | 0006814 | biological_process | sodium ion transport |
C | 0010181 | molecular_function | FMN binding |
C | 0016020 | cellular_component | membrane |
C | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
D | 0005886 | cellular_component | plasma membrane |
D | 0006811 | biological_process | monoatomic ion transport |
D | 0006814 | biological_process | sodium ion transport |
D | 0016020 | cellular_component | membrane |
D | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
E | 0005886 | cellular_component | plasma membrane |
E | 0006811 | biological_process | monoatomic ion transport |
E | 0006814 | biological_process | sodium ion transport |
E | 0009276 | cellular_component | Gram-negative-bacterium-type cell wall |
E | 0016020 | cellular_component | membrane |
E | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
E | 0022904 | biological_process | respiratory electron transport chain |
F | 0005886 | cellular_component | plasma membrane |
F | 0006811 | biological_process | monoatomic ion transport |
F | 0006814 | biological_process | sodium ion transport |
F | 0009055 | molecular_function | electron transfer activity |
F | 0016020 | cellular_component | membrane |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
F | 0046872 | molecular_function | metal ion binding |
F | 0051536 | molecular_function | iron-sulfur cluster binding |
F | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
F | 0071949 | molecular_function | FAD binding |
Functional Information from PROSITE/UniProt
site_id | PS00089 |
Number of Residues | 22 |
Details | RIBORED_LARGE Ribonucleotide reductase large subunit signature. WlaVfpamfw.GMYNaggQAiaA |
Chain | Residue | Details |
B | TRP61-ALA82 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI5 |
Number of Residues | 177 |
Details | Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00426","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Modified residue: {"description":"FMN phosphoryl threonine","evidences":[{"source":"HAMAP-Rule","id":"MF_00426","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22366169","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | Modified residue: {"description":"FMN phosphoryl threonine","evidences":[{"source":"HAMAP-Rule","id":"MF_00427","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22366169","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00427","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 100 |
Details | Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00428","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 120 |
Details | Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00429","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI16 |
Number of Residues | 94 |
Details | Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"HAMAP-Rule","id":"MF_00430","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI17 |
Number of Residues | 140 |
Details | Domain: {"description":"FAD-binding FR-type","evidences":[{"source":"HAMAP-Rule","id":"MF_00430","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI18 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00430","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15379571","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI19 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00430","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |