UniProtKB - B2HN69 (CAR_MYCMM)

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History
Entry version 62 (23 May 2018)
Sequence version 1 (10 Jun 2008)
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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

V_max=
2.32 µmol/min/mg enzyme with benzoate as substrate
1 Publication
Manual assertion based on experiment inⁱ
- Ref.2
  "Carboxylic acid reductase is a versatile enzyme for the conversion of fatty acids into fuels and chemical commodities."
  Akhtar M.K., Turner N.J., Jones P.R.
  Proc. Natl. Acad. Sci. U.S.A. 110:87-92(2013) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, BIOTECHNOLOGY.

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

ATP binding Source: UniProtKB-KW
oxidoreductase activity Source: UniProtKB-KW
phosphopantetheine binding Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

fatty acid metabolic process Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Biological process	Fatty acid metabolism, Lipid metabolism
Ligand	ATP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

BRENDAⁱ	1.2.99.6 3506

BRENDAⁱ

1.2.99.6 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
Organismⁱ	Mycobacterium marinum (strain ATCC BAA-535 / M)
Taxonomic identifierⁱ	216594 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Terrabacteria group › Actinobacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium marinum
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 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)serinePROSITE-ProRule annotation		1

Keywords - PTMⁱ

Phosphopantetheine, Phosphoprotein

Proteomic databases

PRIDEⁱ	B2HN69

PRIDEⁱ

B2HN69

Interactionⁱ

Protein-protein interaction databases

STRINGⁱ	216594.MMAR_2117

STRINGⁱ

216594.MMAR_2117

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	716 – 725	Combined sources	10
Helixⁱ	735 – 739	Combined sources	5
Beta strandⁱ	748 – 750	Combined sources	3
Helixⁱ	751 – 753	Combined sources	3
Helixⁱ	756 – 758	Combined sources	3
Helixⁱ	762 – 767	Combined sources	6
Helixⁱ	768 – 770	Combined sources	3
Beta strandⁱ	780 – 784	Combined sources	5
Helixⁱ	789 – 804	Combined sources	16
Beta strandⁱ	808 – 813	Combined sources	6
Beta strandⁱ	815 – 817	Combined sources	3
Helixⁱ	818 – 828	Combined sources	11
Helixⁱ	834 – 847	Combined sources	14
Beta strandⁱ	848 – 852	Combined sources	5
Helixⁱ	858 – 861	Combined sources	4
Helixⁱ	864 – 873	Combined sources	10
Beta strandⁱ	876 – 879	Combined sources	4
Beta strandⁱ	886 – 888	Combined sources	3
Helixⁱ	890 – 897	Combined sources	8
Helixⁱ	899 – 908	Combined sources	10
Beta strandⁱ	910 – 913	Combined sources	4
Beta strandⁱ	916 – 921	Combined sources	6
Helixⁱ	922 – 927	Combined sources	6
Helixⁱ	930 – 932	Combined sources	3
Beta strandⁱ	935 – 937	Combined sources	3
Helixⁱ	939 – 942	Combined sources	4
Beta strandⁱ	944 – 947	Combined sources	4
Beta strandⁱ	949 – 951	Combined sources	3
Helixⁱ	954 – 974	Combined sources	21
Beta strandⁱ	978 – 983	Combined sources	6
Beta strandⁱ	985 – 987	Combined sources	3
Beta strandⁱ	990 – 992	Combined sources	3
Helixⁱ	1001 – 1012	Combined sources	12
Beta strandⁱ	1014 – 1017	Combined sources	4
Beta strandⁱ	1035 – 1037	Combined sources	3
Helixⁱ	1038 – 1048	Combined sources	11
Helixⁱ	1050 – 1052	Combined sources	3
Beta strandⁱ	1053 – 1060	Combined sources	8
Helixⁱ	1071 – 1080	Combined sources	10
Beta strandⁱ	1086 – 1090	Combined sources	5
Helixⁱ	1091 – 1103	Combined sources	13
Helixⁱ	1107 – 1111	Combined sources	5
Helixⁱ	1115 – 1121	Combined sources	7
Helixⁱ	1136 – 1144	Combined sources	9
Turnⁱ	1148 – 1151	Combined sources	4
Helixⁱ	1158 – 1170	Combined sources	13

3D structure databases

ProteinModelPortalⁱ	B2HN69
SMRⁱ	B2HN69
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	651 – 726	CarrierPROSITE-ProRule 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

Sequence similaritiesⁱ

Belongs to the carboxylic acid reductase family.Curated

Phylogenomic databases

eggNOGⁱ	ENOG4105E4E Bacteria COG1022 LUCA COG3320 LUCA
HOGENOMⁱ	HOG000046493
KEGG Orthology (KO) More...KOⁱ	K12421
OMAⁱ	YSASETH
Database of Orthologous Groups More...OrthoDBⁱ	POG091H0900

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd05235 SDR_e1, 1 hit
Gene3Dⁱ	1.10.1200.10, 1 hit
InterProⁱ	View 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
Pfam protein domain database More...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

Sequenceⁱ

Sequence statusⁱ: Complete.

B2HN69-1 [UniParc]FASTA Add 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

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CP000854 Genomic DNA Translation: ACC40567.1
NCBI Reference Sequences More...RefSeqⁱ	WP_012393886.1, NC_010612.1

Genome annotation databases

EnsemblBacteriaⁱ	ACC40567; ACC40567; MMAR_2117
KEGGⁱ	mmi:MMAR_2117

Protein	Similar proteins		Species	Score	Length
B2HN69	Fatty-acid-CoA ligase FadD9		MYCUA		1174
Fatty-acid-CoA ligase		Mycobacterium ulcerans subsp. shinshuense		1174
Fatty-acid-CoA ligase FadD9		MYCL1		1174
Long-chain-fatty-acid--CoA ligase		Mycobacterium pseudoshottsii JCM 15466		1174
UPI000358A950		Mycobacterium sp. 012931		1174
+4

Protein	Similar proteins		Species	Score	Length
B2HN69	Carboxylic acid reductase	)	NOCIO		1174
Oxidoreductase		Mycobacterium sp. 1274761.0		1166
Oxidoreductase		Mycobacterium sp. TBL 1200985		1171
UPI0006853B0D		Nocardia higoensis		1179
UPI00024A26E8		Mycolicibacterium tusciae		1165
+465

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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	[»]
ProteinModelPortalⁱ	B2HN69
SMRⁱ	B2HN69
ModBaseⁱ	Search...
MobiDBⁱ	Search...

STRINGⁱ	216594.MMAR_2117

PRIDEⁱ	B2HN69

Structural Biology Knowledgebase	Search...

BRENDAⁱ	1.2.99.6 3506

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:	May 23, 2018
	This is version 62 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

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UniProtKB - B2HN69 (CAR_MYCMM)

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Carboxylic acid reductase

car

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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Functionⁱ

Kineticsⁱ

pH dependenceⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Pathology & Biotechⁱ

Biotechnological useⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ