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Protein

Carboxylic acid reductase

Gene

car

Organism
Mycobacterium marinum (strain ATCC BAA-535 / M)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.1 Publication

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.1 Publication

Catalytic activityi

An aldehyde + NADP+ + AMP + diphosphate + H2O = a carboxylate + NADPH + ATP.1 Publication

Cofactori

pantetheine 4'-phosphate1 PublicationNote: Binds 1 phosphopantetheine covalently.1 Publication

Kineticsi

  1. KM=362 µM for benzoate1 Publication
  2. KM=48 µM for NADPH1 Publication
  3. KM=115 µM for ATP1 Publication
  1. Vmax=2.32 µmol/min/mg enzyme with benzoate as substrate1 Publication

pH dependencei

Optimum pH is 7.5.1 Publication

Temperature dependencei

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.1 Publication

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processFatty acid metabolism, Lipid metabolism
LigandATP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

BRENDAi1.2.99.6 3506

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxylic acid reductase1 Publication (EC:1.2.1.-)
Short name:
CAR1 Publication
Alternative name(s):
ATP/NADPH-dependent carboxylic acid reductase
Fatty acid reductase
Gene namesi
Name:car
Synonyms:fadD9
Ordered Locus Names:MMAR_2117
OrganismiMycobacterium marinum (strain ATCC BAA-535 / M)
Taxonomic identifieri216594 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000001190 Componenti: Chromosome

Pathology & Biotechi

Biotechnological usei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004254481 – 1174Carboxylic acid reductaseAdd BLAST1174

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei685O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PRIDEiB2HN69

Interactioni

Protein-protein interaction databases

STRINGi216594.MMAR_2117

Structurei

Secondary structure

11174
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi716 – 725Combined sources10
Helixi735 – 739Combined sources5
Beta strandi748 – 750Combined sources3
Helixi751 – 753Combined sources3
Helixi756 – 758Combined sources3
Helixi762 – 767Combined sources6
Helixi768 – 770Combined sources3
Beta strandi780 – 784Combined sources5
Helixi789 – 804Combined sources16
Beta strandi808 – 813Combined sources6
Beta strandi815 – 817Combined sources3
Helixi818 – 828Combined sources11
Helixi834 – 847Combined sources14
Beta strandi848 – 852Combined sources5
Helixi858 – 861Combined sources4
Helixi864 – 873Combined sources10
Beta strandi876 – 879Combined sources4
Beta strandi886 – 888Combined sources3
Helixi890 – 897Combined sources8
Helixi899 – 908Combined sources10
Beta strandi910 – 913Combined sources4
Beta strandi916 – 921Combined sources6
Helixi922 – 927Combined sources6
Helixi930 – 932Combined sources3
Beta strandi935 – 937Combined sources3
Helixi939 – 942Combined sources4
Beta strandi944 – 947Combined sources4
Beta strandi949 – 951Combined sources3
Helixi954 – 974Combined sources21
Beta strandi978 – 983Combined sources6
Beta strandi985 – 987Combined sources3
Beta strandi990 – 992Combined sources3
Helixi1001 – 1012Combined sources12
Beta strandi1014 – 1017Combined sources4
Beta strandi1035 – 1037Combined sources3
Helixi1038 – 1048Combined sources11
Helixi1050 – 1052Combined sources3
Beta strandi1053 – 1060Combined sources8
Helixi1071 – 1080Combined sources10
Beta strandi1086 – 1090Combined sources5
Helixi1091 – 1103Combined sources13
Helixi1107 – 1111Combined sources5
Helixi1115 – 1121Combined sources7
Helixi1136 – 1144Combined sources9
Turni1148 – 1151Combined sources4
Helixi1158 – 1170Combined sources13

3D structure databases

ProteinModelPortaliB2HN69
SMRiB2HN69
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini651 – 726CarrierPROSITE-ProRule annotationAdd BLAST76

Domaini

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.By similarity

Sequence similaritiesi

Belongs to the carboxylic acid reductase family.Curated

Phylogenomic databases

eggNOGiENOG4105E4E Bacteria
COG1022 LUCA
COG3320 LUCA
HOGENOMiHOG000046493
KOiK12421
OMAiYSASETH
OrthoDBiPOG091H0900

Family and domain databases

CDDicd05235 SDR_e1, 1 hit
Gene3Di1.10.1200.10, 1 hit
InterProiView protein in InterPro
IPR036736 ACP-like_sf
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
IPR013120 Male_sterile_NAD-bd
IPR036291 NAD(P)-bd_dom_sf
IPR020806 PKS_PP-bd
IPR009081 PP-bd_ACP
IPR010080 Thioester_reductase-like_dom
PfamiView protein in Pfam
PF00501 AMP-binding, 1 hit
PF07993 NAD_binding_4, 1 hit
PF00550 PP-binding, 1 hit
SMARTiView protein in SMART
SM00823 PKS_PP, 1 hit
SUPFAMiSSF47336 SSF47336, 1 hit
SSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR01746 Thioester-redct, 1 hit
PROSITEiView protein in PROSITE
PS00061 ADH_SHORT, 1 hit
PS00455 AMP_BINDING, 1 hit
PS50075 CARRIER, 1 hit

Sequencei

Sequence statusi: Complete.

B2HN69-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPITREERL ERRIQDLYAN DPQFAAAKPA TAITAAIERP GLPLPQIIET
60 70 80 90 100
VMTGYADRPA LAQRSVEFVT DAGTGHTTLR LLPHFETISY GELWDRISAL
110 120 130 140 150
ADVLSTEQTV KPGDRVCLLG FNSVDYATID MTLARLGAVA VPLQTSAAIT
160 170 180 190 200
QLQPIVAETQ PTMIAASVDA LADATELALS GQTATRVLVF DHHRQVDAHR
210 220 230 240 250
AAVESARERL AGSAVVETLA EAIARGDVPR GASAGSAPGT DVSDDSLALL
260 270 280 290 300
IYTSGSTGAP KGAMYPRRNV ATFWRKRTWF EGGYEPSITL NFMPMSHVMG
310 320 330 340 350
RQILYGTLCN GGTAYFVAKS DLSTLFEDLA LVRPTELTFV PRVWDMVFDE
360 370 380 390 400
FQSEVDRRLV DGADRVALEA QVKAEIRNDV LGGRYTSALT GSAPISDEMK
410 420 430 440 450
AWVEELLDMH LVEGYGSTEA GMILIDGAIR RPAVLDYKLV DVPDLGYFLT
460 470 480 490 500
DRPHPRGELL VKTDSLFPGY YQRAEVTADV FDADGFYRTG DIMAEVGPEQ
510 520 530 540 550
FVYLDRRNNV LKLSQGEFVT VSKLEAVFGD SPLVRQIYIY GNSARAYLLA
560 570 580 590 600
VIVPTQEALD AVPVEELKAR LGDSLQEVAK AAGLQSYEIP RDFIIETTPW
610 620 630 640 650
TLENGLLTGI RKLARPQLKK HYGELLEQIY TDLAHGQADE LRSLRQSGAD
660 670 680 690 700
APVLVTVCRA AAALLGGSAS DVQPDAHFTD LGGDSLSALS FTNLLHEIFD
710 720 730 740 750
IEVPVGVIVS PANDLQALAD YVEAARKPGS SRPTFASVHG ASNGQVTEVH
760 770 780 790 800
AGDLSLDKFI DAATLAEAPR LPAANTQVRT VLLTGATGFL GRYLALEWLE
810 820 830 840 850
RMDLVDGKLI CLVRAKSDTE ARARLDKTFD SGDPELLAHY RALAGDHLEV
860 870 880 890 900
LAGDKGEADL GLDRQTWQRL ADTVDLIVDP AALVNHVLPY SQLFGPNALG
910 920 930 940 950
TAELLRLALT SKIKPYSYTS TIGVADQIPP SAFTEDADIR VISATRAVDD
960 970 980 990 1000
SYANGYSNSK WAGEVLLREA HDLCGLPVAV FRCDMILADT TWAGQLNVPD
1010 1020 1030 1040 1050
MFTRMILSLA ATGIAPGSFY ELAADGARQR AHYDGLPVEF IAEAISTLGA
1060 1070 1080 1090 1100
QSQDGFHTYH VMNPYDDGIG LDEFVDWLNE SGCPIQRIAD YGDWLQRFET
1110 1120 1130 1140 1150
ALRALPDRQR HSSLLPLLHN YRQPERPVRG SIAPTDRFRA AVQEAKIGPD
1160 1170
KDIPHVGAPI IVKYVSDLRL LGLL
Length:1,174
Mass (Da):127,797
Last modified:June 10, 2008 - v1
Checksum:i18E2B5C6B0528AB1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000854 Genomic DNA Translation: ACC40567.1
RefSeqiWP_012393886.1, NC_010612.1

Genome annotation databases

EnsemblBacteriaiACC40567; ACC40567; MMAR_2117
KEGGimmi:MMAR_2117

Similar proteinsi

Entry informationi

Entry nameiCAR_MYCMM
AccessioniPrimary (citable) accession number: B2HN69
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 19, 2014
Last sequence update: June 10, 2008
Last modified: May 23, 2018
This is version 62 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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