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UniProtKB - B2HN69 (CAR_MYCMM)

Entry version 76 (29 Sep 2021)
Sequence version 1 (10 Jun 2008)
Previous versions | rss
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Protein

Carboxylic acid reductase

Gene

car

Organism
Mycobacterium marinum (strain ATCC BAA-535 / M)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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 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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

pantetheine 4'-phosphateUniRule annotation1 PublicationNote: Binds 1 phosphopantetheine covalently.UniRule annotation1 Publication

<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

  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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei297AMPUniRule annotation1
Binding sitei392AMPUniRule annotation1
Binding sitei418AMPUniRule annotation1
Binding sitei491AMPUniRule annotation1
Binding sitei512AMPUniRule annotation1
Binding sitei612AMPUniRule annotation1
Binding sitei814NADPUniRule annotationCombined sources1 Publication1
Binding sitei824NADPUniRule annotationCombined sources1 Publication1
Binding sitei956NADPUniRule annotationCombined sources1 Publication1
Binding sitei960NADPUniRule annotationCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi413 – 414AMPUniRule annotation2
Nucleotide bindingi503 – 506AMPUniRule annotation4
Nucleotide bindingi787 – 791NADPCombined sources1 Publication5
Nucleotide bindingi854 – 855NADPUniRule annotationCombined sources1 Publication2
Nucleotide bindingi880 – 882NADPUniRule annotationCombined sources1 Publication3
Nucleotide bindingi919 – 920NADPCombined sources1 Publication2

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.2.1.30, 3506

<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 subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:carUniRule annotation
Synonyms:fadD9
Ordered Locus Names:MMAR_2117
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMycobacterium marinum (strain ATCC BAA-535 / M)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri216594 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001190 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<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

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

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004254481 – 1174Carboxylic acid reductaseAdd BLAST1174

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei685O-(pantetheine 4'-phosphoryl)serineUniRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

<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

STRING: functional protein association networks

More...STRINGi		216594.MMAR_2117

<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

11174
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		B2HN69

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini651 – 726CarrierUniRule annotationAdd BLAST76

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<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

Belongs to the ATP-dependent AMP-binding enzyme family. Carboxylic acid reductase subfamily.UniRule annotationCurated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG1022, Bacteria
COG3320, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_009549_0_0_11

Identification of Orthologs from Complete Genome Data

More...OMAi		QVIVHAA

Database of Orthologous Groups

More...OrthoDBi		572620at2

Family and domain databases

Conserved Domains Database

More...CDDi		cd05235, SDR_e1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.1200.10, 1 hit
3.40.50.12780, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_02247, Carbox_acid_reduct, 1 hit

Integrated resource of protein families, domains and functional sites

More...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

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

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00823, PKS_PP, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47336, SSF47336, 1 hit
SSF51735, SSF51735, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01746, Thioester-redct, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00061, ADH_SHORT, 1 hit
PS00455, AMP_BINDING, 1 hit
PS50075, CARRIER, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i18E2B5C6B0528AB1
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
CP000854 Genomic DNA Translation: ACC40567.1

NCBI Reference Sequences

More...RefSeqi		WP_012393886.1, NC_010612.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		ACC40567; ACC40567; MMAR_2117

Database of genes from NCBI RefSeq genomes

More...GeneIDi		64260821

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmi:MMAR_2117

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

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

3D structure databases

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 entryMethodResolution (Å)ChainPositionsPDBsum
5MSOX-ray1.20A1-1174[»]
5MSUX-ray1.74A/B/C1-1174[»]
SMRiB2HN69
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi216594.MMAR_2117

Genome annotation databases

EnsemblBacteriaiACC40567; ACC40567; MMAR_2117
GeneIDi64260821
KEGGimmi:MMAR_2117

Phylogenomic databases

eggNOGiCOG1022, Bacteria
COG3320, Bacteria
HOGENOMiCLU_009549_0_0_11
OMAiQVIVHAA
OrthoDBi572620at2

Enzyme and pathway databases

BRENDAi1.2.1.30, 3506

Family and domain databases

CDDicd05235, SDR_e1, 1 hit
Gene3Di1.10.1200.10, 1 hit
3.40.50.12780, 1 hit
HAMAPiMF_02247, Carbox_acid_reduct, 1 hit
InterProiView 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
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

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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 subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCAR_MYCMM
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: B2HN69
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated 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.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<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

Keywords - Technical termi

3D-structure, 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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