CAR_NEUCR
ID CAR_NEUCR Reviewed; 1052 AA.
AC Q7RW48;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Carboxylic acid reductase {ECO:0000303|PubMed:27917101};
DE Short=CAR {ECO:0000303|PubMed:27917101};
DE EC=1.2.1.- {ECO:0000269|PubMed:11946054, ECO:0000269|PubMed:27917101, ECO:0000269|PubMed:29515539, ECO:0000269|PubMed:4389863};
DE EC=1.2.1.30 {ECO:0000269|PubMed:11946054, ECO:0000269|PubMed:27917101, ECO:0000269|PubMed:29515539, ECO:0000269|PubMed:4389863};
DE AltName: Full=Aryl aldehyde:NADP oxidoreductase {ECO:0000303|PubMed:4389863};
GN ORFNames=NCU05000;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=4389863; DOI=10.1111/j.1432-1033.1969.tb00543.x;
RA Gross G.G., Zenk M.H.;
RT "[Reduction of aromatic acids to aldehydes and alcohols in the cell-free
RT system. 1. Purification and properties of aryl-aldehyde: NADP-
RT oxidoreductase from Neurospora crassa].";
RL Eur. J. Biochem. 8:413-419(1969).
RN [3]
RP CATALYTIC ACTIVITY.
RX PubMed=11946054; DOI=10.1016/0014-5793(71)80172-2;
RA Gross G.G.;
RT "Stoichiometric studies on aryl-aldehyde: NADP oxidoreductase from
RT Neurospra crassa.";
RL FEBS Lett. 17:309-311(1971).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=27917101; DOI=10.1002/adsc.201600914;
RA Schwendenwein D., Fiume G., Weber H., Rudroff F., Winkler M.;
RT "Selective enzymatic transformation to aldehydes in vivo by fungal
RT carboxylate reductase from Neurospora crassa.";
RL Adv. Synth. Catal. 358:3414-3421(2016).
RN [5]
RP FUNCTION, DOMAIN, CATALYTIC ACTIVITY, AND MUTAGENESIS OF SER-183; GLY-184;
RP PRO-189; PRO-234; HIS-237; PRO-285; GLY-310; THR-336; ASP-405; ARG-422;
RP GLU-433; GLU-441; GLY-457; SER-595; GLY-691; GLY-694; TYR-844; LYS-848;
RP ARG-870; GLY-882; PRO-904 AND TRP-978.
RX PubMed=29515539; DOI=10.3389/fmicb.2018.00250;
RA Stolterfoht H., Steinkellner G., Schwendenwein D., Pavkov-Keller T.,
RA Gruber K., Winkler M.;
RT "Identification of Key Residues for Enzymatic Carboxylate Reduction.";
RL Front. Microbiol. 9:250-250(2018).
CC -!- FUNCTION: Carboxylic acid reductase that shows a broad range of
CC substrate specificity towards aromatic acids, especially to phenyl
CC carboxylic and phenyl acrylic acids, to convert them into their
CC respective aldehydes (PubMed:4389863, PubMed:11946054, PubMed:27917101,
CC PubMed:29515539). Also able to use aliphatic acids as substrates
CC (PubMed:29515539). {ECO:0000269|PubMed:11946054,
CC ECO:0000269|PubMed:27917101, ECO:0000269|PubMed:29515539,
CC ECO:0000269|PubMed:4389863}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + an aromatic aldehyde + diphosphate + NADP(+) = an
CC aromatic carboxylate + ATP + H(+) + NADPH; Xref=Rhea:RHEA:19229,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:33855, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:91007, ChEBI:CHEBI:456215; EC=1.2.1.30;
CC Evidence={ECO:0000269|PubMed:11946054, ECO:0000269|PubMed:27917101,
CC ECO:0000269|PubMed:29515539, ECO:0000269|PubMed:4389863};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19231;
CC Evidence={ECO:0000269|PubMed:11946054, ECO:0000269|PubMed:27917101,
CC ECO:0000269|PubMed:29515539, ECO:0000269|PubMed:4389863};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a carboxylate + ATP + H(+) + NADPH = AMP + an aldehyde +
CC diphosphate + NADP(+); Xref=Rhea:RHEA:50916, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:29515539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50917;
CC Evidence={ECO:0000269|PubMed:29515539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + benzoate + H(+) + NADPH = AMP + benzaldehyde +
CC diphosphate + NADP(+); Xref=Rhea:RHEA:68868, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16150, ChEBI:CHEBI:17169, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:27917101};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68869;
CC Evidence={ECO:0000269|PubMed:27917101};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamate + ATP + H(+) + NADPH = (E)-cinnamaldehyde + AMP
CC + diphosphate + NADP(+); Xref=Rhea:RHEA:68872, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15669, ChEBI:CHEBI:16731, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:27917101};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68873;
CC Evidence={ECO:0000269|PubMed:27917101};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + NADPH + piperonylate = AMP + diphosphate +
CC NADP(+) + piperonal; Xref=Rhea:RHEA:68876, ChEBI:CHEBI:8240,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:180537,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:27917101};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68877;
CC Evidence={ECO:0000269|PubMed:27917101};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + NADPH + salicylate = AMP + diphosphate + NADP(+)
CC + salicylaldehyde; Xref=Rhea:RHEA:68880, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16008, ChEBI:CHEBI:30616, ChEBI:CHEBI:30762,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:27917101};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68881;
CC Evidence={ECO:0000269|PubMed:27917101};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxybenzoate + ATP + H(+) + NADPH = 3-hydroxybenzaldehyde
CC + AMP + diphosphate + NADP(+); Xref=Rhea:RHEA:68884,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16193, ChEBI:CHEBI:16207,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:27917101};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68885;
CC Evidence={ECO:0000269|PubMed:27917101};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methoxybenzoate + ATP + H(+) + NADPH = 2-methoxybenzaldehyde
CC + AMP + diphosphate + NADP(+); Xref=Rhea:RHEA:68888,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59128,
CC ChEBI:CHEBI:172139, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:27917101};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68889;
CC Evidence={ECO:0000269|PubMed:27917101};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methoxybenzoate + ATP + H(+) + NADPH = 3-methoxybenzaldehyde
CC + AMP + diphosphate + NADP(+); Xref=Rhea:RHEA:68892,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:136805,
CC ChEBI:CHEBI:180538, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:27917101};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68893;
CC Evidence={ECO:0000269|PubMed:27917101};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoate + ATP + H(+) + NADPH = 4-hydroxybenzaldehyde
CC + AMP + diphosphate + NADP(+); Xref=Rhea:RHEA:68896,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17597, ChEBI:CHEBI:17879,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:27917101};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68897;
CC Evidence={ECO:0000269|PubMed:27917101};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methoxybenzoate + ATP + H(+) + NADPH = 4-methoxybenzaldehyde
CC + AMP + diphosphate + NADP(+); Xref=Rhea:RHEA:68900,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16639, ChEBI:CHEBI:28235,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:27917101};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68901;
CC Evidence={ECO:0000269|PubMed:27917101};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phenylpropanoate + ATP + H(+) + NADPH = 3-phenylpropanal +
CC AMP + diphosphate + NADP(+); Xref=Rhea:RHEA:68904, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:39940,
CC ChEBI:CHEBI:51057, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:27917101};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68905;
CC Evidence={ECO:0000269|PubMed:27917101};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + NADPH + picolinate = AMP + diphosphate + NADP(+)
CC + picolinal; Xref=Rhea:RHEA:68908, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:38184,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:73012,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:27917101};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68909;
CC Evidence={ECO:0000269|PubMed:27917101};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + NADPH + propanoate = AMP + diphosphate + NADP(+)
CC + propanal; Xref=Rhea:RHEA:68912, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17153, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:29515539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68913;
CC Evidence={ECO:0000269|PubMed:29515539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + butanoate + H(+) + NADPH = AMP + butanal + diphosphate +
CC NADP(+); Xref=Rhea:RHEA:68916, ChEBI:CHEBI:15378, ChEBI:CHEBI:15743,
CC ChEBI:CHEBI:17968, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:29515539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68917;
CC Evidence={ECO:0000269|PubMed:29515539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + NADPH + pentanoate = AMP + diphosphate + NADP(+)
CC + pentanal; Xref=Rhea:RHEA:68920, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:31011, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:84069,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:29515539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68921;
CC Evidence={ECO:0000269|PubMed:29515539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + hexanoate + NADPH = AMP + diphosphate + hexanal +
CC NADP(+); Xref=Rhea:RHEA:68924, ChEBI:CHEBI:15378, ChEBI:CHEBI:17120,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:88528, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:29515539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68925;
CC Evidence={ECO:0000269|PubMed:29515539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + heptanoate + NADPH = AMP + diphosphate + heptanal
CC + NADP(+); Xref=Rhea:RHEA:68928, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32362, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:34787, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:29515539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68929;
CC Evidence={ECO:0000269|PubMed:29515539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + NADPH + octanoate = AMP + diphosphate + NADP(+) +
CC octanal; Xref=Rhea:RHEA:68932, ChEBI:CHEBI:15378, ChEBI:CHEBI:17935,
CC ChEBI:CHEBI:25646, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:29515539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68933;
CC Evidence={ECO:0000269|PubMed:29515539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + NADPH + nonanoate = AMP + diphosphate + NADP(+) +
CC nonanal; Xref=Rhea:RHEA:68936, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:32361, ChEBI:CHEBI:33019, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:84268, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:29515539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68937;
CC Evidence={ECO:0000269|PubMed:29515539};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:4389863};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=167 uM for salicylic acid {ECO:0000269|PubMed:4389863};
CC KM=152 uM for ATP {ECO:0000269|PubMed:4389863};
CC KM=445 uM for cinnamic acid {ECO:0000269|PubMed:27917101};
CC KM=173 uM for piperonylic acid {ECO:0000269|PubMed:27917101};
CC Vmax=2.33 umol/min/mg enzyme towards cinnamic acid
CC {ECO:0000269|PubMed:27917101};
CC Vmax=3.7 umol/min/mg enzyme towards piperonylic acid
CC {ECO:0000269|PubMed:27917101};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:4389863};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:4389863};
CC -!- DOMAIN: The NRPS-like carboxylic acid reductase (CAR) has an unusual
CC domain architecture (A-T-R), with the adenylation domain A activating
CC and thioesterifying the carboxylic acid which is then channeled through
CC the phosphopantetheine arm of the T domain, the thioester reductase
CC domain R reducing the carboxylic acid to the corresponding aldehyde.
CC {ECO:0000269|PubMed:29515539}.
CC -!- SIMILARITY: Belongs to the adenylate-forming reductase family.
CC {ECO:0000305}.
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DR EMBL; CM002241; EAA26584.1; -; Genomic_DNA.
DR RefSeq; XP_955820.1; XM_950727.2.
DR SMR; Q7RW48; -.
DR STRING; 5141.EFNCRP00000001459; -.
DR EnsemblFungi; EAA26584; EAA26584; NCU05000.
DR GeneID; 3871967; -.
DR KEGG; ncr:NCU05000; -.
DR VEuPathDB; FungiDB:NCU05000; -.
DR HOGENOM; CLU_002220_0_0_1; -.
DR InParanoid; Q7RW48; -.
DR Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; NADP; Nucleotide-binding; Oxidoreductase; Phosphopantetheine;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1052
FT /note="Carboxylic acid reductase"
FT /id="PRO_0000454508"
FT DOMAIN 560..643
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 21..344
FT /note="Adenylation (A) domain"
FT /evidence="ECO:0000305|PubMed:29515539"
FT REGION 684..979
FT /note="Carboxylic acid reductase (R) domain"
FT /evidence="ECO:0000305|PubMed:29515539"
FT BINDING 334..335
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 339
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 419..422
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 693..696
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 718
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 774..776
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 814
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 844
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 848
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT MOD_RES 595
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MUTAGEN 183
FT /note="S->A: Decreases CAR activity."
FT /evidence="ECO:0000269|PubMed:29515539"
FT MUTAGEN 184
FT /note="G->A: Reduces the solubility of the protein."
FT /evidence="ECO:0000269|PubMed:29515539"
FT MUTAGEN 189
FT /note="P->A: Enhances the specific activity with hexanoic
FT acid."
FT /evidence="ECO:0000269|PubMed:29515539"
FT MUTAGEN 234
FT /note="P->A: Enhances the specific activity with aliphatic
FT acids."
FT /evidence="ECO:0000269|PubMed:29515539"
FT MUTAGEN 237
FT /note="H->A: Abolishes CAR activity."
FT /evidence="ECO:0000269|PubMed:29515539"
FT MUTAGEN 285
FT /note="P->A: Increases the activity for the reduction of
FT piperonylic acid and aliphatic acids."
FT /evidence="ECO:0000269|PubMed:29515539"
FT MUTAGEN 310
FT /note="G->A: Does not affect activity with cinnamic acid,
FT but a decreases activity with piperonylic and hexanoic
FT acid."
FT /evidence="ECO:0000269|PubMed:29515539"
FT MUTAGEN 336
FT /note="T->A: Decreases CAR activity and retains activity
FT mainly on piperonylic acid."
FT /evidence="ECO:0000269|PubMed:29515539"
FT MUTAGEN 405
FT /note="D->A: Decreases CAR activity and shows activity
FT solely on piperonylic acid."
FT /evidence="ECO:0000269|PubMed:29515539"
FT MUTAGEN 422
FT /note="R->A: Decreases CAR activity."
FT /evidence="ECO:0000269|PubMed:29515539"
FT MUTAGEN 433
FT /note="E->A: Abolishes CAR activity."
FT /evidence="ECO:0000269|PubMed:29515539"
FT MUTAGEN 441
FT /note="E->A: Enhances the specific activity with hexanoic
FT acid."
FT /evidence="ECO:0000269|PubMed:29515539"
FT MUTAGEN 457
FT /note="G->A: Decreases CAR activity, but enhances the
FT specific activity with hexanoic acid."
FT /evidence="ECO:0000269|PubMed:29515539"
FT MUTAGEN 595
FT /note="S->A: Abolishes CAR activity."
FT /evidence="ECO:0000269|PubMed:29515539"
FT MUTAGEN 691
FT /note="G->A: Leads to only residual activity."
FT /evidence="ECO:0000269|PubMed:29515539"
FT MUTAGEN 694
FT /note="G->A: Leads to only residual activity."
FT /evidence="ECO:0000269|PubMed:29515539"
FT MUTAGEN 844
FT /note="Y->A: Abolishes CAR activity."
FT /evidence="ECO:0000269|PubMed:29515539"
FT MUTAGEN 848
FT /note="K->A: Abolishes CAR activity."
FT /evidence="ECO:0000269|PubMed:29515539"
FT MUTAGEN 870
FT /note="R->A: Reduces the solubility of the protein."
FT /evidence="ECO:0000269|PubMed:29515539"
FT MUTAGEN 882
FT /note="G->A: Decreases CAR activity."
FT /evidence="ECO:0000269|PubMed:29515539"
FT MUTAGEN 904
FT /note="P->A: Reduces the solubility of the protein and
FT decreases CAR activity."
FT /evidence="ECO:0000269|PubMed:29515539"
FT MUTAGEN 978
FT /note="W->A: Reduces the solubility of the protein."
FT /evidence="ECO:0000269|PubMed:29515539"
SQ SEQUENCE 1052 AA; 117751 MW; 4823A586E93AC8E4 CRC64;
MSQQQNPPYG RRLILDIIKE RALNEPNREW VSVPRSSDPK DGWKILTYLD AYNGINRVAH
KLTQVCGAAA PGSFPTVAYI GPNDVRYLVF ALGAVKAGYK ALFISTRNSA EAQVNLFELT
NCNVLVFDQS YKATVQPWLH EREMTAILAL PADEWFPADQ EDFPYNKTFE EAEWDPLMVL
HTSGSTGFPK PIVARQGMLA VADQFHNLPP REDGKLMWIV EMSKRAKRLM HPMPLFHAAG
MYISMLMIHY WDTPGALGIG ERPLSSDLVL DYIEYADVEG MILPPAILEE LSRDEKAIQS
LQKLNFVSFG GGNLAPEAGD RLVENNVTLC NLISATEFTP FPFYWQYDQK LWRYFNFDTD
LFGIDWRLHD GESTYEQVIV RKDKHPGLQG FFYTFPDSSE YSTKDLYKRH PTHEDFWIYQ
GRADNIIVFS NGEKLNPITI EETLQGHPKV MGAVVVGTNR FQPALIIEPV EHPETEEGRK
ALLDEIWPTV VRVNKETVAH GQIGRQYMAL STPGKPFLRA GKGTVLRPGT INMYKAEIDK
IYEDAEKGVA TDEVPKLDLS SSDALIVSIE KLFETSLNAP KLEADTDFFT AGVDSMQVIT
ASRLIRAGLA AAGVNIEASA LATRVIYGNP TPKRLADYLL SIVNKDSNQG TLDNEHHVME
ALVEKYTRDL PTPKQNKPAP ADEGQVVVIT GTTGGIGSYL IDICSSSSRV SKIICLNRSE
DGKARQTASS SGRGLSTDFS KCEFYHADMS RADLGLGPEV YSRLLSEVDR VIHNQWPVNF
NIAVESFEPH IRGCRNLVDF SYKADKNVPI VFVSSIGTVD RWHDEDRIVP EASLDDLSLA
AGGYGQSKLV SSLIFDKAAE VSGVPTEVVR VGQVAGPSSE KGYWNKQEWL PSIVASSAYL
GVLPDSLGQM TTIDWTPIEA IAKLLLEVSG VIDNVPLDKI NGYFHGVNPE RTSWSALAPA
VQEYYGDRIQ KIVPLDEWLE ALEKSQEKAE DVTRNPGIKL IDTYRTWSEG YKKGTKFVPL
DMTRTKEYSK TMREMHAVTP ELMKNWCRQW NF
