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: | Q6N8W1 |
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| Protein Name: | Putative branched-chain amino acid transport system ATP-binding protein |
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| Length: | 590 |
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| Molecular Weight: | 62825.00 |
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| Species: | Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) [258594] |
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| Number of TMSs: | 9 |
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| Substrate |
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1: MPRWLPILLF AAVMTALPLI PGIPPFWIVL LDNIGLAALV AMGLVLLTGV GGLTSFGQAA
61: FCGFGAYTTA YITTVYGISP WLALPASLVV AGIAAVLLGL MTVRLSGHYL PLGTIAWGIA
121: LYYLFSKLDF LGRNDGISRV PPLSIGPIDM YDPHTIYFVI WAMVLISAVL TMNLLDSRTG
181: RAIRALRRGH VAAEAFGVQT ARAKLLVFIY AAVLAGLSGW LYAHFQRNVN PTPFGPQAGI
241: EYLFIAVVGG AGYVWGGVLG AAIVIILKEV LQGYLPLLFG GQGQLEIIVF GILLVVLLQL
301: APGGVWPWLA NLVPLKFRRA VTGNADGLPA RERVGGSTTA PLLKVERARK QFGGVVAVND
361: VSFEVNAAEI VALIGPNGAG KSTTFNLITG ILTTTGGRIE VHGKPVDNTP PQEVVKLGIA
421: RTFQHVKLVP DMTVLENVAI GAHLRGRSGA ITSMLRFDRG DEAKLLAEAA RQIERVGLGA
481: EIDQLAGSLS LGQQRIVEIA RALCADPELL LLDEPAAGLR HMEKQRLAAL LRQLKDSGMS
541: VLLVEHDMGF VMDLADRIVV LDFGTRIAEG TPDAIKTNPD VIKAYLGALA