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Carboxylic acid reductase (CAR) (EC 1.2.1.-) (ATP/NADPH-dependent carboxylic acid reductase) (Fatty acid reductase)

 CAR_MYCMM               Reviewed;        1174 AA.
B2HN69;
19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
23-MAY-2018, entry version 62.
RecName: Full=Carboxylic acid reductase {ECO:0000303|PubMed:23248280};
Short=CAR {ECO:0000303|PubMed:23248280};
EC=1.2.1.-;
AltName: Full=ATP/NADPH-dependent carboxylic acid reductase;
AltName: Full=Fatty acid reductase;
Name=car; Synonyms=fadD9; OrderedLocusNames=MMAR_2117;
Mycobacterium marinum (strain ATCC BAA-535 / M).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium.
NCBI_TaxID=216594;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-535 / M;
PubMed=18403782; DOI=10.1101/gr.075069.107;
Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T.,
Churcher C., Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N.,
Jagels K., Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L.,
Brosch R., Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
"Insights from the complete genome sequence of Mycobacterium marinum
on the evolution of Mycobacterium tuberculosis.";
Genome Res. 18:729-741(2008).
[2]
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND BIOTECHNOLOGY.
PubMed=23248280; DOI=10.1073/pnas.1216516110;
Akhtar M.K., Turner N.J., Jones P.R.;
"Carboxylic acid reductase is a versatile enzyme for the conversion of
fatty acids into fuels and chemical commodities.";
Proc. Natl. Acad. Sci. U.S.A. 110:87-92(2013).
-!- FUNCTION: Catalyzes the reduction of a wide range of aliphatic
fatty acids (C6-C18) into their corresponding aldehydes, by using
ATP for energy to drive the reaction. Can also reduce benzoate to
benzaldehyde. Has a preference for NADPH over NADH as the electron
donor. {ECO:0000269|PubMed:23248280}.
-!- CATALYTIC ACTIVITY: An aldehyde + NADP(+) + AMP + diphosphate +
H(2)O = a carboxylate + NADPH + ATP.
{ECO:0000269|PubMed:23248280}.
-!- COFACTOR:
Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
Evidence={ECO:0000305|PubMed:23248280};
Note=Binds 1 phosphopantetheine covalently.
{ECO:0000305|PubMed:23248280};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=362 uM for benzoate {ECO:0000269|PubMed:23248280};
KM=48 uM for NADPH {ECO:0000269|PubMed:23248280};
KM=115 uM for ATP {ECO:0000269|PubMed:23248280};
Vmax=2.32 umol/min/mg enzyme with benzoate as substrate
{ECO:0000269|PubMed:23248280};
pH dependence:
Optimum pH is 7.5. {ECO:0000269|PubMed:23248280};
Temperature dependence:
Displays in vitro half-lives of 73, 70, and 48 hours at 26, 30,
and 37 degrees Celsius, respectively, indicating it is a
relatively stable enzyme. {ECO:0000269|PubMed:23248280};
-!- DOMAIN: The N-terminal domain likely catalyzes substrate
activation by formation of an initial acyl-AMP intermediate, the
central region contains the phosphopantetheine attachment site,
and the C-terminal domain catalyzes the reduction by NADPH of the
intermediate thioester formed from the attack of the
phosphopantetheine thiol at the carbonyl carbon of acyl-AMP.
{ECO:0000250}.
-!- BIOTECHNOLOGY: This enzyme can be applied to the microbial
production of fatty alkanes and fatty alcohols that have numerous
applications as fuels, fragrances, emollients, plasticizers,
thickeners, and detergents. Thus, together with complementing
enzymes, the broad substrate specificity and kinetic
characteristics of Car opens the road for direct and tailored
enzyme-catalyzed conversion of lipids into user-ready chemical
commodities. {ECO:0000269|PubMed:23248280}.
-!- MISCELLANEOUS: The conversion of fatty acid into aldehyde involves
three key steps: adenylation of the bound fatty acid substrate to
form an AMP-fatty acyl complex, formation of a thioester linkage
between the fatty acyl moiety and the phosphopantetheine
prosthetic group, and reduction of the thioester intermediate to
the aldehyde. {ECO:0000305|PubMed:23248280}.
-!- SIMILARITY: Belongs to the carboxylic acid reductase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CP000854; ACC40567.1; -; Genomic_DNA.
RefSeq; WP_012393886.1; NC_010612.1.
PDB; 5MSO; X-ray; 1.20 A; A=1-1174.
PDB; 5MSU; X-ray; 1.74 A; A/B/C=1-1174.
PDBsum; 5MSO; -.
PDBsum; 5MSU; -.
ProteinModelPortal; B2HN69; -.
SMR; B2HN69; -.
STRING; 216594.MMAR_2117; -.
PRIDE; B2HN69; -.
EnsemblBacteria; ACC40567; ACC40567; MMAR_2117.
KEGG; mmi:MMAR_2117; -.
eggNOG; ENOG4105E4E; Bacteria.
eggNOG; COG1022; LUCA.
eggNOG; COG3320; LUCA.
HOGENOM; HOG000046493; -.
KO; K12421; -.
OMA; YSASETH; -.
OrthoDB; POG091H0900; -.
BRENDA; 1.2.99.6; 3506.
Proteomes; UP000001190; Chromosome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
CDD; cd05235; SDR_e1; 1.
Gene3D; 1.10.1200.10; -; 1.
InterPro; IPR036736; ACP-like_sf.
InterPro; IPR020845; AMP-binding_CS.
InterPro; IPR000873; AMP-dep_Synth/Lig.
InterPro; IPR013120; Male_sterile_NAD-bd.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020806; PKS_PP-bd.
InterPro; IPR009081; PP-bd_ACP.
InterPro; IPR010080; Thioester_reductase-like_dom.
Pfam; PF00501; AMP-binding; 1.
Pfam; PF07993; NAD_binding_4; 1.
Pfam; PF00550; PP-binding; 1.
SMART; SM00823; PKS_PP; 1.
SUPFAM; SSF47336; SSF47336; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR01746; Thioester-redct; 1.
PROSITE; PS00061; ADH_SHORT; 1.
PROSITE; PS00455; AMP_BINDING; 1.
PROSITE; PS50075; CARRIER; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Fatty acid metabolism;
Lipid metabolism; NADP; Nucleotide-binding; Oxidoreductase;
Phosphopantetheine; Phosphoprotein; Reference proteome.
CHAIN 1 1174 Carboxylic acid reductase.
/FTId=PRO_0000425448.
DOMAIN 651 726 Carrier. {ECO:0000255|PROSITE-
ProRule:PRU00258}.
MOD_RES 685 685 O-(pantetheine 4'-phosphoryl)serine.
{ECO:0000255|PROSITE-ProRule:PRU00258}.
HELIX 716 725 {ECO:0000244|PDB:5MSU}.
HELIX 735 739 {ECO:0000244|PDB:5MSO}.
STRAND 748 750 {ECO:0000244|PDB:5MSO}.
HELIX 751 753 {ECO:0000244|PDB:5MSO}.
HELIX 756 758 {ECO:0000244|PDB:5MSO}.
HELIX 762 767 {ECO:0000244|PDB:5MSO}.
HELIX 768 770 {ECO:0000244|PDB:5MSO}.
STRAND 780 784 {ECO:0000244|PDB:5MSO}.
HELIX 789 804 {ECO:0000244|PDB:5MSO}.
STRAND 808 813 {ECO:0000244|PDB:5MSO}.
STRAND 815 817 {ECO:0000244|PDB:5MSO}.
HELIX 818 828 {ECO:0000244|PDB:5MSO}.
HELIX 834 847 {ECO:0000244|PDB:5MSO}.
STRAND 848 852 {ECO:0000244|PDB:5MSO}.
HELIX 858 861 {ECO:0000244|PDB:5MSO}.
HELIX 864 873 {ECO:0000244|PDB:5MSO}.
STRAND 876 879 {ECO:0000244|PDB:5MSO}.
STRAND 886 888 {ECO:0000244|PDB:5MSO}.
HELIX 890 897 {ECO:0000244|PDB:5MSO}.
HELIX 899 908 {ECO:0000244|PDB:5MSO}.
STRAND 910 913 {ECO:0000244|PDB:5MSO}.
STRAND 916 921 {ECO:0000244|PDB:5MSO}.
HELIX 922 927 {ECO:0000244|PDB:5MSO}.
HELIX 930 932 {ECO:0000244|PDB:5MSO}.
STRAND 935 937 {ECO:0000244|PDB:5MSO}.
HELIX 939 942 {ECO:0000244|PDB:5MSO}.
STRAND 944 947 {ECO:0000244|PDB:5MSO}.
STRAND 949 951 {ECO:0000244|PDB:5MSO}.
HELIX 954 974 {ECO:0000244|PDB:5MSO}.
STRAND 978 983 {ECO:0000244|PDB:5MSO}.
STRAND 985 987 {ECO:0000244|PDB:5MSU}.
STRAND 990 992 {ECO:0000244|PDB:5MSO}.
HELIX 1001 1012 {ECO:0000244|PDB:5MSO}.
STRAND 1014 1017 {ECO:0000244|PDB:5MSO}.
STRAND 1035 1037 {ECO:0000244|PDB:5MSU}.
HELIX 1038 1048 {ECO:0000244|PDB:5MSO}.
HELIX 1050 1052 {ECO:0000244|PDB:5MSO}.
STRAND 1053 1060 {ECO:0000244|PDB:5MSO}.
HELIX 1071 1080 {ECO:0000244|PDB:5MSO}.
STRAND 1086 1090 {ECO:0000244|PDB:5MSO}.
HELIX 1091 1103 {ECO:0000244|PDB:5MSO}.
HELIX 1107 1111 {ECO:0000244|PDB:5MSO}.
HELIX 1115 1121 {ECO:0000244|PDB:5MSO}.
HELIX 1136 1144 {ECO:0000244|PDB:5MSO}.
TURN 1148 1151 {ECO:0000244|PDB:5MSO}.
HELIX 1158 1170 {ECO:0000244|PDB:5MSO}.
SEQUENCE 1174 AA; 127797 MW; 18E2B5C6B0528AB1 CRC64;
MSPITREERL ERRIQDLYAN DPQFAAAKPA TAITAAIERP GLPLPQIIET VMTGYADRPA
LAQRSVEFVT DAGTGHTTLR LLPHFETISY GELWDRISAL ADVLSTEQTV KPGDRVCLLG
FNSVDYATID MTLARLGAVA VPLQTSAAIT QLQPIVAETQ PTMIAASVDA LADATELALS
GQTATRVLVF DHHRQVDAHR AAVESARERL AGSAVVETLA EAIARGDVPR GASAGSAPGT
DVSDDSLALL IYTSGSTGAP KGAMYPRRNV ATFWRKRTWF EGGYEPSITL NFMPMSHVMG
RQILYGTLCN GGTAYFVAKS DLSTLFEDLA LVRPTELTFV PRVWDMVFDE FQSEVDRRLV
DGADRVALEA QVKAEIRNDV LGGRYTSALT GSAPISDEMK AWVEELLDMH LVEGYGSTEA
GMILIDGAIR RPAVLDYKLV DVPDLGYFLT DRPHPRGELL VKTDSLFPGY YQRAEVTADV
FDADGFYRTG DIMAEVGPEQ FVYLDRRNNV LKLSQGEFVT VSKLEAVFGD SPLVRQIYIY
GNSARAYLLA VIVPTQEALD AVPVEELKAR LGDSLQEVAK AAGLQSYEIP RDFIIETTPW
TLENGLLTGI RKLARPQLKK HYGELLEQIY TDLAHGQADE LRSLRQSGAD APVLVTVCRA
AAALLGGSAS DVQPDAHFTD LGGDSLSALS FTNLLHEIFD IEVPVGVIVS PANDLQALAD
YVEAARKPGS SRPTFASVHG ASNGQVTEVH AGDLSLDKFI DAATLAEAPR LPAANTQVRT
VLLTGATGFL GRYLALEWLE RMDLVDGKLI CLVRAKSDTE ARARLDKTFD SGDPELLAHY
RALAGDHLEV LAGDKGEADL GLDRQTWQRL ADTVDLIVDP AALVNHVLPY SQLFGPNALG
TAELLRLALT SKIKPYSYTS TIGVADQIPP SAFTEDADIR VISATRAVDD SYANGYSNSK
WAGEVLLREA HDLCGLPVAV FRCDMILADT TWAGQLNVPD MFTRMILSLA ATGIAPGSFY
ELAADGARQR AHYDGLPVEF IAEAISTLGA QSQDGFHTYH VMNPYDDGIG LDEFVDWLNE
SGCPIQRIAD YGDWLQRFET ALRALPDRQR HSSLLPLLHN YRQPERPVRG SIAPTDRFRA
AVQEAKIGPD KDIPHVGAPI IVKYVSDLRL LGLL


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