| Evidence_82157 |
TIGR01034 HMM |
None - {{∅}} |
True - {{t}} |
Unconfirmed presence |
|
| Evidence_82158 |
PF01941 HMM |
None - {{∅}} |
None - {{∅}} |
Unexplained |
|
| Evidence_82153 |
TIGR00936 HMM |
None - {{∅}} |
None - {{∅}} |
Unexplained |
|
| Evidence_82154 |
GenProp0757 GENPROP |
None - {{∅}} |
True - {{t}} |
Unconfirmed presence |
|
| Component_54394 |
S-ribosylhomocysteine lyase |
None - {{∅}} |
True - {{t}} |
Unconfirmed presence |
|
| Component_54395 |
methylthioadenosine nucleosidase/adenosylhomocysteine nucleosidase |
None - {{∅}} |
True - {{t}} |
Unconfirmed presence |
|
| Evidence_75386 |
PF02664 HMM |
None - {{∅}} |
True - {{t}} |
Unconfirmed presence |
|
| Evidence_75387 |
TIGR01704 HMM |
None - {{∅}} |
True - {{t}} |
Unconfirmed presence |
|
| Component_60605 |
SAH to homocysteine |
None - {{∅}} |
True - {{t}} |
Unconfirmed presence |
|
| GenProp0789 |
homocysteine regeneration from S-adenosylhomocysteine~S-adenosylmethionine (SAM) is used in cells as a methyl donor by a large guild of methyltransferases, leaving S-adenosylhomocysteine (SAH). SAH can be cleaved in one step to adenosine and homocysteine by adenosylhomocysteinase (EC 3.3.1.1). The homocysteine can then be used to regenerate methionine. Alternatively, it can be cleaved in two steps. First adenine is removed by adenosylhomocysteine nucleosidase (EC 3.2.2.9, a fascinating enzyme that, with a different bound cofactor, acts instead in the pathway of methionine salvage from methylthioadenosine - see TIGR01704) to leave S-ribosylhomocysteine. Next, S-ribosylhomocysteinase acts to produce homocysteine and 4,5-dihydroxypentan-2,3-dione, which cyclizes spontaneously and binds borate to become autoinducer-2 (AI-2), a quorum-sensing molecule produced and recognized by a wide range of bacteria. This property represents the presence at least one of these two mechanisms to regenerate homocysteine. |
None - {{∅}} |
True - {{t}} |
Unconfirmed presence |
|
| GenProp0757 |
quorum-sensing, autoinducer-2 system~S-ribosylhomocysteine lyase, 4.4.1.21, is LuxS, an iron(2+)-containing protein. Its immediate product, 4,5-dihydroxypentan-2,3-dione, cyclizes spontaneously and binds borate to become autoinducer-2 (AI-2), a quorum-sensing molecule produced and recognized by a wide range of bacteria. LuxS serves as a marker for this system, while MTA/SAH nucleosidase is essential both for this and other systems. Many clade-specific proteins interact with this system but are not currently represented as part of this genome property. |
None - {{∅}} |
True - {{t}} |
Unconfirmed presence |
|
| Component_60608 |
methionine adenosyltransferase |
None - {{∅}} |
True - {{t}} |
Unconfirmed presence |
|