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UniProtKB - B2HN69 (CAR_MYCMM)
Protein
Carboxylic acid reductase
Gene
car
Organism
Mycobacterium marinum (strain ATCC BAA-535 / M)
Status
Functioni
Catalyzes the ATP- and NADPH-dependent reduction of carboxylic acids to the corresponding aldehydes (PubMed:23248280).
Catalyzes the reduction of a wide range of aliphatic fatty acids (C6-C18) into their corresponding aldehydes. Can also reduce benzoate to benzaldehyde. Has a preference for NADPH over NADH as the electron donor (PubMed:23248280).
1 PublicationMiscellaneous
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
- a carboxylate + ATP + H+ + NADPH = AMP + an aldehyde + diphosphate + NADP+UniRule annotation1 Publication
Cofactori
pantetheine 4'-phosphateUniRule annotation1 PublicationNote: Binds 1 phosphopantetheine covalently.UniRule annotation1 Publication
Kineticsi
- KM=362 µM for benzoate1 Publication
- KM=48 µM for NADPH1 Publication
- KM=115 µM for ATP1 Publication
- 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
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 297 | AMPUniRule annotation | 1 | |
Binding sitei | 392 | AMPUniRule annotation | 1 | |
Binding sitei | 418 | AMPUniRule annotation | 1 | |
Binding sitei | 491 | AMPUniRule annotation | 1 | |
Binding sitei | 512 | AMPUniRule annotation | 1 | |
Binding sitei | 612 | AMPUniRule annotation | 1 | |
Binding sitei | 814 | NADPUniRule annotationCombined sources1 Publication | 1 | |
Binding sitei | 824 | NADPUniRule annotationCombined sources1 Publication | 1 | |
Binding sitei | 956 | NADPUniRule annotationCombined sources1 Publication | 1 | |
Binding sitei | 960 | NADPUniRule annotationCombined sources1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 413 – 414 | AMPUniRule annotation | 2 | |
Nucleotide bindingi | 503 – 506 | AMPUniRule annotation | 4 | |
Nucleotide bindingi | 787 – 791 | NADPCombined sources1 Publication | 5 | |
Nucleotide bindingi | 854 – 855 | NADPUniRule annotationCombined sources1 Publication | 2 | |
Nucleotide bindingi | 880 – 882 | NADPUniRule annotationCombined sources1 Publication | 3 | |
Nucleotide bindingi | 919 – 920 | NADPCombined sources1 Publication | 2 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- oxidoreductase activity Source: UniProtKB-KW
- phosphopantetheine binding Source: InterPro
GO - Biological processi
- fatty acid metabolic process Source: UniProtKB-KW
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Fatty acid metabolism, Lipid metabolism |
Ligand | ATP-binding, NADP, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 1.2.1.30, 3506 |
Names & Taxonomyi
Protein namesi | Recommended name: Carboxylic acid reductase1 PublicationUniRule annotation (EC:1.2.1.-UniRule annotation)Short name: CAR1 PublicationUniRule annotation Alternative name(s): ATP/NADPH-dependent carboxylic acid reductaseUniRule annotation Fatty acid reductase |
Gene namesi | Name:carUniRule annotation Synonyms:fadD9 Ordered Locus Names:MMAR_2117 |
Organismi | Mycobacterium marinum (strain ATCC BAA-535 / M) |
Taxonomic identifieri | 216594 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › |
Proteomesi |
|
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000425448 | 1 – 1174 | Carboxylic acid reductaseAdd BLAST | 1174 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 685 | O-(pantetheine 4'-phosphoryl)serineUniRule annotation | 1 |
Keywords - PTMi
Phosphopantetheine, PhosphoproteinStructurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | B2HN69 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 651 – 726 | CarrierUniRule annotationAdd BLAST | 76 |
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). Large-scale domain motions occur between the adenylation and thiolation states. Phosphopantetheine binding alters the orientation of a key Asp, resulting in a productive orientation of the bound nicotinamide. This ensures that further reduction of the aldehyde product does not occur (PubMed:28719588).By similarity1 Publication
Sequence similaritiesi
Belongs to the ATP-dependent AMP-binding enzyme family. Carboxylic acid reductase subfamily.UniRule annotationCurated
Phylogenomic databases
eggNOGi | COG1022, Bacteria COG3320, Bacteria |
HOGENOMi | CLU_009549_0_0_11 |
OMAi | QVIVHAA |
OrthoDBi | 572620at2 |
Family and domain databases
CDDi | cd05235, SDR_e1, 1 hit |
Gene3Di | 1.10.1200.10, 1 hit 3.40.50.12780, 1 hit |
HAMAPi | MF_02247, Carbox_acid_reduct, 1 hit |
InterProi | View protein in InterPro IPR036736, ACP-like_sf IPR020845, AMP-binding_CS IPR000873, AMP-dep_Synth/Lig IPR042099, ANL_N_sf IPR013120, Far_NAD-bd IPR036291, NAD(P)-bd_dom_sf IPR020806, PKS_PP-bd IPR009081, PP-bd_ACP IPR010080, Thioester_reductase-like_dom |
Pfami | View protein in Pfam PF00501, AMP-binding, 1 hit PF07993, NAD_binding_4, 1 hit PF00550, PP-binding, 1 hit |
SMARTi | View protein in SMART SM00823, PKS_PP, 1 hit |
SUPFAMi | SSF47336, SSF47336, 1 hit SSF51735, SSF51735, 1 hit |
TIGRFAMsi | TIGR01746, Thioester-redct, 1 hit |
PROSITEi | View protein in PROSITE PS00061, ADH_SHORT, 1 hit PS00455, AMP_BINDING, 1 hit PS50075, CARRIER, 1 hit |
i Sequence
Sequence statusi: Complete.
B2HN69-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP000854 Genomic DNA Translation: ACC40567.1 |
RefSeqi | WP_012393886.1, NC_010612.1 |
Genome annotation databases
EnsemblBacteriai | ACC40567; ACC40567; MMAR_2117 |
GeneIDi | 64260821 |
KEGGi | mmi:MMAR_2117 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP000854 Genomic DNA Translation: ACC40567.1 |
RefSeqi | WP_012393886.1, NC_010612.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
5MSO | X-ray | 1.20 | A | 1-1174 | [»] | |
5MSU | X-ray | 1.74 | A/B/C | 1-1174 | [»] | |
SMRi | B2HN69 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 216594.MMAR_2117 |
Genome annotation databases
EnsemblBacteriai | ACC40567; ACC40567; MMAR_2117 |
GeneIDi | 64260821 |
KEGGi | mmi:MMAR_2117 |
Phylogenomic databases
eggNOGi | COG1022, Bacteria COG3320, Bacteria |
HOGENOMi | CLU_009549_0_0_11 |
OMAi | QVIVHAA |
OrthoDBi | 572620at2 |
Enzyme and pathway databases
BRENDAi | 1.2.1.30, 3506 |
Family and domain databases
CDDi | cd05235, SDR_e1, 1 hit |
Gene3Di | 1.10.1200.10, 1 hit 3.40.50.12780, 1 hit |
HAMAPi | MF_02247, Carbox_acid_reduct, 1 hit |
InterProi | View protein in InterPro IPR036736, ACP-like_sf IPR020845, AMP-binding_CS IPR000873, AMP-dep_Synth/Lig IPR042099, ANL_N_sf IPR013120, Far_NAD-bd IPR036291, NAD(P)-bd_dom_sf IPR020806, PKS_PP-bd IPR009081, PP-bd_ACP IPR010080, Thioester_reductase-like_dom |
Pfami | View protein in Pfam PF00501, AMP-binding, 1 hit PF07993, NAD_binding_4, 1 hit PF00550, PP-binding, 1 hit |
SMARTi | View protein in SMART SM00823, PKS_PP, 1 hit |
SUPFAMi | SSF47336, SSF47336, 1 hit SSF51735, SSF51735, 1 hit |
TIGRFAMsi | TIGR01746, Thioester-redct, 1 hit |
PROSITEi | View protein in PROSITE PS00061, ADH_SHORT, 1 hit PS00455, AMP_BINDING, 1 hit PS50075, CARRIER, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CAR_MYCMM | |
Accessioni | B2HN69Primary (citable) accession number: B2HN69 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 19, 2014 |
Last sequence update: | June 10, 2008 | |
Last modified: | September 29, 2021 | |
This is version 76 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families