3.A.1.4.11 The phenylpropeneoid uptake porter, CouPSTW. The purple photosynthetic bacterium Rhodopseudomonas palustris is able
to grow photoheterotrophically under anaerobic conditions on a range of
phenylpropeneoid lignin monomers, including coumarate, ferulate, caffeate, and cinnamate.
RPA1789 (CouP) is the periplasmic binding-protein component of the ABC uptake system (CouPSTU). CouP binds a range of
phenylpropeneoid ligands with Kd values in the nanomolar range. The
crystal structure of CouP with ferulate as the bound ligand shows H-bond
interactions between the 4-OH group of the aromatic ring with His309
and Gln305. H-bonds are also made between the carboxyl group on the
ferulate side chain and Arg197, Ser222, and Thr102 (Salmon et al. 2013). Within the same operon are a diguanylate cyclase (Q6N8W3) and a phenylacetate-CoA ligase (Q6N8W5).
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Accession Number: | Q6N8W4 |
Protein Name: | Putative branched-chain amino acid transport system substrate-binding protein |
Length: | 385 |
Molecular Weight: | 40884.00 |
Species: | Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) [258594] |
Number of TMSs: | 2 |
Substrate |
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1: MTKFKLSATA IAVALALPGL SGAALAETNE ITIGITVTTT GPAAALGIPE RNALEFVAKE
61: IGGHPLKVIV LDDGGDPTAA TTNARRFVTE SKADVIMGSS VTPPTVAVSN VANEAQVPHI
121: ALAPLPITPE RAKWSVAMPQ PIPIMGKVLY EHMKKNNIKT VGYIGYSDSY GDLWFNDLKK
181: QGEAMGLKIV AEERFARPDT SVAGQVLKLV AANPDAILVG ASGTAAALPQ TSLRERGYKG
241: LIYQTHGAAS MDFIRIAGKS AEGVLMASGP VMDPEGQDDS ALTKKPGLEL NTAYEAKYGP
301: NSRSQFAAHS FDAFKVLERV VPVALKTAKP GTQEFREAIR KALVSEKDIA ASQGVYSFTE
361: TDRYGLDDRS RILLTVKDGK YVMVK