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Entry version 78 (02 Jun 2021)
Sequence version 1 (24 Nov 2009)
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Protein

Carnitine monooxygenase reductase subunit

Gene

cntB

Organism
Acinetobacter baumannii (strain ATCC 19606 / DSM 30007 / CIP 70.34 / JCM 6841 / NBRC 109757 / NCIMB 12457 / NCTC 12156 / 81)
Status
Reviewed-Annotation score:

Annotation score:4 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

Converts carnitine to trimethylamine and malic semialdehyde.

UniRule annotation1 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

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: carnitine metabolism

This protein is involved in the pathway carnitine metabolism, which is part of Amine and polyamine metabolism.UniRule annotation1 Publication
View all proteins of this organism that are known to be involved in the pathway carnitine metabolism and in Amine and polyamine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi267Iron-sulfur (2Fe-2S)UniRule annotation1
Metal bindingi272Iron-sulfur (2Fe-2S)UniRule annotation1
Metal bindingi275Iron-sulfur (2Fe-2S)UniRule annotation1
Metal bindingi305Iron-sulfur (2Fe-2S)UniRule annotation1

<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

GO - Biological processi

<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
Ligand2Fe-2S, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD, NADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-18570

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.14.13.239, 98

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00117

<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:
Carnitine monooxygenase reductase subunitUniRule annotationCurated (EC:1.14.13.239UniRule annotation1 Publication)
Alternative name(s):
Carnitine monooxygenase beta subunitUniRule annotationCurated
<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:cntB1 Publication
ORF Names:F911_03117Imported, HMPREF0010_01351Imported
<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>OrganismiAcinetobacter baumannii (strain ATCC 19606 / DSM 30007 / CIP 70.34 / JCM 6841 / NBRC 109757 / NCIMB 12457 / NCTC 12156 / 81)
<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 identifieri575584 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex
<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
  • UP000005740 <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: Unassembled WGS sequence

<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 in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mutant cannot grow on carnitine as a sole carbon and energy source, whereas the growth on succinate is not affected. Mutation abolishes trimethylamine formation from carnitine.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_00004426881 – 318Carnitine monooxygenase reductase subunitAdd BLAST318

<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

Composed of an oxygenase subunit (cntA) and a reductase subunit (cntB).

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

3D structure databases

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

More...
SMRi
D0C9N8

Database of comparative protein structure models

More...
ModBasei
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>Domaini5 – 107FAD-binding FR-typeUniRule annotationAdd BLAST103
Domaini233 – 3182Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST86

<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 PDR/VanB family. CntB subfamily.UniRule annotationCurated

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00207, fer2, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.10.20.30, 1 hit
3.40.50.80, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_02098, Carnitine_monoox_B, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036010, 2Fe-2S_ferredoxin-like_sf
IPR001041, 2Fe-2S_ferredoxin-type
IPR006058, 2Fe2S_fd_BS
IPR012675, Beta-grasp_dom_sf
IPR039003, Carnitine_monoox_B
IPR008333, Cbr1-like_FAD-bd_dom
IPR017927, FAD-bd_FR_type
IPR039261, FNR_nucleotide-bd
IPR001433, OxRdtase_FAD/NAD-bd
IPR000951, Ph_dOase_redase
IPR017938, Riboflavin_synthase-like_b-brl

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00970, FAD_binding_6, 1 hit
PF00111, Fer2, 1 hit
PF00175, NAD_binding_1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00409, PHDIOXRDTASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52343, SSF52343, 1 hit
SSF54292, SSF54292, 1 hit
SSF63380, SSF63380, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00197, 2FE2S_FER_1, 1 hit
PS51085, 2FE2S_FER_2, 1 hit
PS51384, FAD_FR, 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.

D0C9N8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASHYEMFPA VVTRVEQLTP LIKRFTFKRQ DGQNFPRFSG GSHIIVKMNE
60 70 80 90 100
QLSNAYSLMS CTQDLSTYQV CVRKDVEGKG GSVFMHDQCN EGCEIQISEP
110 120 130 140 150
KNLFPLAETG NKHILIAGGI GITPFLPQMD ELAARGAEYE LHYAYRSPEH
160 170 180 190 200
AALLDELTQK HAGHVFSYVD SEGSMLNLDE LISSQPKGTH VYVCGPKPMI
210 220 230 240 250
DAVIDCCNKH RYRDEYIHWE QFASTVPEDG EAFTVVLAKS NQEIEVQSNQ
260 270 280 290 300
TILQAIETLN IDVECLCREG VCGTCETAIL EGEAEHFDQY LSDAEKASQK
310
SMMICVSRAK GKKLVLDL
Length:318
Mass (Da):35,538
Last modified:November 24, 2009 - 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:i9D5C7FE49B27D0EF
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
GG704573 Genomic DNA Translation: EEX03957.1
APRG01000016 Genomic DNA Translation: ENW73703.1

NCBI Reference Sequences

More...
RefSeqi
WP_000146428.1, NZ_KB849991.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
EEX03957; EEX03957; HMPREF0010_01351

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|575584.18.peg.3257

<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
GG704573 Genomic DNA Translation: EEX03957.1
APRG01000016 Genomic DNA Translation: ENW73703.1
RefSeqiWP_000146428.1, NZ_KB849991.1

3D structure databases

SMRiD0C9N8
ModBaseiSearch...

Genome annotation databases

EnsemblBacteriaiEEX03957; EEX03957; HMPREF0010_01351
PATRICifig|575584.18.peg.3257

Enzyme and pathway databases

UniPathwayiUPA00117
BioCyciMetaCyc:MONOMER-18570
BRENDAi1.14.13.239, 98

Family and domain databases

CDDicd00207, fer2, 1 hit
Gene3Di3.10.20.30, 1 hit
3.40.50.80, 1 hit
HAMAPiMF_02098, Carnitine_monoox_B, 1 hit
InterProiView protein in InterPro
IPR036010, 2Fe-2S_ferredoxin-like_sf
IPR001041, 2Fe-2S_ferredoxin-type
IPR006058, 2Fe2S_fd_BS
IPR012675, Beta-grasp_dom_sf
IPR039003, Carnitine_monoox_B
IPR008333, Cbr1-like_FAD-bd_dom
IPR017927, FAD-bd_FR_type
IPR039261, FNR_nucleotide-bd
IPR001433, OxRdtase_FAD/NAD-bd
IPR000951, Ph_dOase_redase
IPR017938, Riboflavin_synthase-like_b-brl
PfamiView protein in Pfam
PF00970, FAD_binding_6, 1 hit
PF00111, Fer2, 1 hit
PF00175, NAD_binding_1, 1 hit
PRINTSiPR00409, PHDIOXRDTASE
SUPFAMiSSF52343, SSF52343, 1 hit
SSF54292, SSF54292, 1 hit
SSF63380, SSF63380, 1 hit
PROSITEiView protein in PROSITE
PS00197, 2FE2S_FER_1, 1 hit
PS51085, 2FE2S_FER_2, 1 hit
PS51384, FAD_FR, 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 nameiCNTB_ACIB2
<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: D0C9N8
<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: December 20, 2017
Last sequence update: November 24, 2009
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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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