EC Number   |
General Information |
Reference |
|---|
   7.3.2.5 | evolution |
ModABC belongs to the family of ATP-binding cassette (ABC) transporters, while PerO is a member of the ArsB/NhaD family |
719720 |
| 7.3.2.5 | evolution |
ModABC belongs to the family of molybdate uptake transporters MolT |
719038 |
| 7.3.2.5 | evolution |
ModABC belongs to the family of molybdate uptake transporters MolT, PerO belongs to the ArsB/NhaD ion transporter family |
719038 |
| 7.3.2.5 | evolution |
WtpABC belongs to the sulfate/tungstate uptake transporter SulT family, overview. ModABC belongs to the family of molybdate uptake transporters MolT |
719038 |
| 7.3.2.5 | malfunction |
an enzyme mutation is sufficient to prevent growth on nitrate without the addition of molybdate to the growth medium |
-, 751611 |
| 7.3.2.5 | malfunction |
during growth under Mo-replete conditions, the wild-type strain accumulates considerably more Mo than the enzyme mutant |
719720 |
| 7.3.2.5 | metabolism |
Campylobacter jejuni possesses a specific, ultra high affinity tungstate transporter that supplies tungsten for incorporation into formate dehydrogenase, in additon to a molybdate/tungstate transporter ModA, EC 3.6.3.29, and also two MoeA paralogues which may explain the formation of both molybdopterin and tungstopterin in this bacterium |
713053 |
| 7.3.2.5 | metabolism |
ModE-like protein regulates both transporters, repressing mod in the presence of both molybdenum and tungsten and tup only in the presence of tungsten. Like other ModE proteins, the Campylobacter jejuni ModE binds DNA through a helix-turn-helix DNA binding domain, but unlike other members of the ModE family it does not have a metal binding domain |
713054 |
| 7.3.2.5 | metabolism |
specific high-affinity ATP-binding cassette (ABC) transporting systems uptake molybdenum and tungsten in the form of soluble oxyanions, molybdate and tungstate. Among them are the bacterial TupABC transporting system, which is highly specific for tungstate and does not transport other anions, and the ModABC system, which can transport both molybdate and tungstate, regulation of the ModABC transport system. TunR proteins participate in protection of the cells from the inhibition by these oxyanions |
-, 734088 |
| 7.3.2.5 | more |
ModC is negatively regulated by the ranscription factors MopA and MopB, overview |
712284 |
