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Entry version 78 (02 Jun 2021)
Sequence version 1 (05 Jul 2004)
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Protein

Carboxylic acid reductase

Gene

car

Organism
Nocardia iowensis
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. Catalyzes the reduction of a very wide range of aliphatic carboxylic acids as well as many aryl carboxylic acids. Aryl carboxylic acid substrates include substituted benzoic acids, phenyl-substituted aliphatic acids, heterocyclic carboxylic acids, and polyaromatic ring carboxylic acids. Cannot reduce benzaldehyde to benzyl alcohol.

4 Publications

Miscellaneous

The conversion of carboxylic acid into aldehyde involves three key steps: adenylation of the bound carboxylic acid substrate to form an AMP-acyl intermediate, formation of a thioester linkage between the 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Is competitively inhibited by anthranilate when using benzoate as substrate.1 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

Vmax is 3 times higher than that of the natural enzyme when recombinant apo-Car is incubated with the purified PPTase Npt and CoA.1 Publication
  1. KM=645 µM for benzoate2 Publications
  2. KM=57.3 µM for ATP2 Publications
  3. KM=29.3 µM for NADPH2 Publications
  4. KM=34.5 µM for (R)---alpha-methyl-4-(2-methylpropyl)-benzeneacetate ((R)-ibuprofen)2 Publications
  5. KM=155 µM for (S)-+-alpha-methyl-4-(2-methylpropyl)-benzeneacetate ((S)-ibuprofen)2 Publications
  1. Vmax=0.902 µmol/min/mg enzyme with benzoate as substrate2 Publications
  2. Vmax=1.33 µmol/min/mg enzyme with (R)---alpha-methyl-4-(2-methylpropyl)-benzeneacetate as substrate2 Publications
  3. Vmax=0.15 µmol/min/mg enzyme with (S)-+-alpha-methyl-4-(2-methylpropyl)-benzeneacetate as substrate2 Publications

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 sitei300AMPUniRule annotationCombined sources1 Publication1
Binding sitei395AMPUniRule annotationCombined sources1 Publication1
Binding sitei421AMPUniRule annotationCombined sources1 Publication1
Binding sitei495AMPUniRule annotationCombined sources1 Publication1
Binding sitei516AMPUniRule annotation1
Binding sitei616AMPUniRule annotationCombined sources1 Publication1
Binding sitei814NADPUniRule annotation1
Binding sitei824NADPUniRule annotation1
Binding sitei920NADP; via carbonyl oxygenUniRule annotation1
Binding sitei956NADPUniRule annotation1
Binding sitei960NADPUniRule annotation1
Binding sitei983NADPUniRule annotation1

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 bindingi416 – 417AMPUniRule annotationCombined sources1 Publication2
Nucleotide bindingi507 – 510AMPUniRule annotationCombined sources1 Publication4
Nucleotide bindingi787 – 790NADPUniRule annotation4
Nucleotide bindingi880 – 882NADPUniRule annotation3

<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>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
LigandATP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-20627

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.2.1.30, 10331

<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
Aryl aldehyde oxidoreductase1 Publication (EC:1.2.1.303 Publications)
<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
<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>OrganismiNocardia iowensis
<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 identifieri204891 [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 lineageiBacteriaActinobacteriaCorynebacterialesNocardiaceaeNocardia

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi689S → A: Loss of catalytic activity. 1 Publication1

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<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_00004254492 – 1174Carboxylic acid reductaseAdd BLAST1173

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 residuei689O-(pantetheine 4'-phosphoryl)serineUniRule annotation1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

4'-phosphopantetheine is transferred from CoA to Ser-689 by Npt.

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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

1 Publication

<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
Q6RKB1

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>Domaini655 – 730CarrierUniRule 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 (PubMed:17102130). 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).2 Publications

<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

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, AMP-dep_Synthh-like_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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q6RKB1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAVDSPDERL QRRIAQLFAE DEQVKAARPL EAVSAAVSAP GMRLAQIAAT
60 70 80 90 100
VMAGYADRPA AGQRAFELNT DDATGRTSLR LLPRFETITY RELWQRVGEV
110 120 130 140 150
AAAWHHDPEN PLRAGDFVAL LGFTSIDYAT LDLADIHLGA VTVPLQASAA
160 170 180 190 200
VSQLIAILTE TSPRLLASTP EHLDAAVECL LAGTTPERLV VFDYHPEDDD
210 220 230 240 250
QRAAFESARR RLADAGSLVI VETLDAVRAR GRDLPAAPLF VPDTDDDPLA
260 270 280 290 300
LLIYTSGSTG TPKGAMYTNR LAATMWQGNS MLQGNSQRVG INLNYMPMSH
310 320 330 340 350
IAGRISLFGV LARGGTAYFA AKSDMSTLFE DIGLVRPTEI FFVPRVCDMV
360 370 380 390 400
FQRYQSELDR RSVAGADLDT LDREVKADLR QNYLGGRFLV AVVGSAPLAA
410 420 430 440 450
EMKTFMESVL DLPLHDGYGS TEAGASVLLD NQIQRPPVLD YKLVDVPELG
460 470 480 490 500
YFRTDRPHPR GELLLKAETT IPGYYKRPEV TAEIFDEDGF YKTGDIVAEL
510 520 530 540 550
EHDRLVYVDR RNNVLKLSQG EFVTVAHLEA VFASSPLIRQ IFIYGSSERS
560 570 580 590 600
YLLAVIVPTD DALRGRDTAT LKSALAESIQ RIAKDANLQP YEIPRDFLIE
610 620 630 640 650
TEPFTIANGL LSGIAKLLRP NLKERYGAQL EQMYTDLATG QADELLALRR
660 670 680 690 700
EAADLPVLET VSRAAKAMLG VASADMRPDA HFTDLGGDSL SALSFSNLLH
710 720 730 740 750
EIFGVEVPVG VVVSPANELR DLANYIEAER NSGAKRPTFT SVHGGGSEIR
760 770 780 790 800
AADLTLDKFI DARTLAAADS IPHAPVPAQT VLLTGANGYL GRFLCLEWLE
810 820 830 840 850
RLDKTGGTLI CVVRGSDAAA ARKRLDSAFD SGDPGLLEHY QQLAARTLEV
860 870 880 890 900
LAGDIGDPNL GLDDATWQRL AETVDLIVHP AALVNHVLPY TQLFGPNVVG
910 920 930 940 950
TAEIVRLAIT ARRKPVTYLS TVGVADQVDP AEYQEDSDVR EMSAVRVVRE
960 970 980 990 1000
SYANGYGNSK WAGEVLLREA HDLCGLPVAV FRSDMILAHS RYAGQLNVQD
1010 1020 1030 1040 1050
VFTRLILSLV ATGIAPYSFY RTDADGNRQR AHYDGLPADF TAAAITALGI
1060 1070 1080 1090 1100
QATEGFRTYD VLNPYDDGIS LDEFVDWLVE SGHPIQRITD YSDWFHRFET
1110 1120 1130 1140 1150
AIRALPEKQR QASVLPLLDA YRNPCPAVRG AILPAKEFQA AVQTAKIGPE
1160 1170
QDIPHLSAPL IDKYVSDLEL LQLL
Length:1,174
Mass (Da):128,346
Last modified:July 5, 2004 - 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:iD95F16957D6F95D8
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
AY495697 Genomic DNA Translation: AAR91681.1

<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
AY495697 Genomic DNA Translation: AAR91681.1

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
5MSCX-ray1.85A1-1174[»]
5MSDX-ray1.71A1-1174[»]
5MSQX-ray1.74A1-1174[»]
SMRiQ6RKB1
ModBaseiSearch...
PDBe-KBiSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-20627
BRENDAi1.2.1.30, 10331

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, AMP-dep_Synthh-like_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_NOCIO
<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: Q6RKB1
<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: July 5, 2004
Last modified: June 2, 2021
This is version 78 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, Direct protein sequencing

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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