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Entry version 51 (08 May 2019)
Sequence version 1 (30 Nov 2010)
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Protein

Flavohemoprotein

Gene

hmpA

Organism
Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia)
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

Flavohemoprotein involved in nitric oxide (NO) detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O2 and NAD(P)H to convert NO to nitrate, which protects the protozoan parasite from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress. May also be involved in O2 detoxification.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 ‘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=22 µM for O21 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei30Involved in heme-bound ligand stabilization and O-O bond activationBy similarity1
    Sitei106Influences the redox potential of the prosthetic heme and FAD groupsBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi107Iron (heme proximal ligand)PROSITE-ProRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei117Charge relay systemBy similarity1
    Active sitei157Charge relay systemBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei211FADBy similarity1
    Sitei449Influences the redox potential of the prosthetic heme and FAD groupsBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi228 – 231FADBy similarity4
    Nucleotide bindingi321 – 326NADPBy similarity6
    Nucleotide bindingi450 – 453FADBy similarity4

    <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
    Biological processDetoxification, Oxygen transport, Transport
    LigandFAD, Flavoprotein, Heme, Iron, Metal-binding, NAD, NADP

    <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_and_taxonomy_section">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:
    Flavohemoprotein
    Alternative name(s):
    Flavohemoglobin
    Short name:
    FlavoHb
    Hemoglobin-like protein
    Nitric oxide dioxygenase (EC:1.14.12.17)
    Short name:
    NO oxygenase
    Short name:
    NOD
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:hmpA
    Synonyms:FLHb
    ORF Names:GL50803_15009
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiGiardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri184922 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaDiplomonadidaHexamitidaeGiardiinaeGiardia
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
    • UP000001548 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    GiardiaDB:GL50803_15009

    <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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004093541 – 458FlavohemoproteinAdd BLAST458

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Expressed at very low levels in untreated trophozoites of the parasite. Expression is markedly stimulated in nitrite-supplemented medium. Induction by nitrite is probably mediated by NO, likely generated upon reduction of nitrite. Also induced in cells grown in the presence of the NO-donors 3,3-bis(aminoethyl)-1-hydroxy-2-oxo-1-triazene (DETA-NONOate), and S-nitrosoglutathione (GSNO).1 Publication

    <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_section">'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_section">'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

    3D structure databases

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

    More...
    SMRi
    E2RTZ4

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    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_and_domains_section">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>Domaini172 – 279FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST108

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 160GlobinBy similarityAdd BLAST160
    Regioni169 – 457ReductaseBy similarityAdd BLAST289
    Regioni312 – 457NAD or NADP-bindingBy similarityAdd BLAST146

    <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

    Consists of two distinct domains; an N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H.

    <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 globin family. Two-domain flavohemoproteins subfamily.PROSITE-ProRule annotation
    In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG3378 Eukaryota
    COG1017 LUCA
    COG1018 LUCA

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    E2RTZ4

    KEGG Orthology (KO)

    More...
    KOi
    K05916

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    EALITHF

    Database of Orthologous Groups

    More...
    OrthoDBi
    696109at2759

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.10.490.10, 2 hits
    3.40.50.80, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR008333 Cbr1-like_FAD-bd_dom
    IPR017927 FAD-bd_FR_type
    IPR039261 FNR_nucleotide-bd
    IPR000971 Globin
    IPR009050 Globin-like_sf
    IPR012292 Globin/Proto
    IPR023950 Hmp
    IPR001433 OxRdtase_FAD/NAD-bd
    IPR017938 Riboflavin_synthase-like_b-brl

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR43396 PTHR43396, 1 hit

    Pfam protein domain database

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

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF46458 SSF46458, 1 hit
    SSF52343 SSF52343, 1 hit
    SSF63380 SSF63380, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51384 FAD_FR, 1 hit
    PS01033 GLOBIN, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

    E2RTZ4-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTLSEDTLRA VEATAGLIAA QGIEFTRAFY ERMLTKNEEL KNIFNLAHQR
    60 70 80 90 100
    TLRQPKALLD SLVAYALNIR RINELYELKG KGLPVPPEHW AELQGFFSAA
    110 120 130 140 150
    ERVANKHTSF GIQPAQYQIV GAHLLATIED RITKDKDILA EWAKAYQFLA
    160 170 180 190 200
    DLFIKREEEI YAATEGCKGG WRQTRTFRVE EKTRVNEIIC KFRLVPAEEG
    210 220 230 240 250
    AGVVEHRPGQ YLAIFVRSPE HFQHQQIRQY SIISAPNSAY YEIAVHRDEK
    260 270 280 290 300
    GTVSRYLHDY VSTGDLLEVA PPYGDFFLRY LEADEQAPAD TQASQEFQML
    310 320 330 340 350
    QSGAINFAAE KTMPIVLISG GIGQTPLLSM LRFLAQKEGK ETARPIFWIH
    360 370 380 390 400
    AAHNSRVRAF KEEVDAIRET ALPSLRVVTF LSEVRATDRE GEDYDFAGRI
    410 420 430 440 450
    NLDRISELTK LEADNANPHY FFVGPTGFMT AVEEQLKTKS VPNSRIHFEM

    FGPFKASH
    Length:458
    Mass (Da):52,003
    Last modified:November 30, 2010 - 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:i1A55B5C1CD2A38CB
    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
    AY132357 Genomic DNA Translation: AAM94640.1
    AACB02000055 Genomic DNA Translation: EDO76804.1

    NCBI Reference Sequences

    More...
    RefSeqi
    XP_001704478.1, XM_001704426.1

    Genome annotation databases

    Ensembl protists genome annotation project

    More...
    EnsemblProtistsi
    EDO76804; EDO76804; GL50803_15009

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    5697339

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    gla:GL50803_15009

    <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
    AY132357 Genomic DNA Translation: AAM94640.1
    AACB02000055 Genomic DNA Translation: EDO76804.1
    RefSeqiXP_001704478.1, XM_001704426.1

    3D structure databases

    SMRiE2RTZ4
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblProtistsiEDO76804; EDO76804; GL50803_15009
    GeneIDi5697339
    KEGGigla:GL50803_15009

    Organism-specific databases

    EuPathDBiGiardiaDB:GL50803_15009

    Phylogenomic databases

    eggNOGiKOG3378 Eukaryota
    COG1017 LUCA
    COG1018 LUCA
    InParanoidiE2RTZ4
    KOiK05916
    OMAiEALITHF
    OrthoDBi696109at2759

    Family and domain databases

    Gene3Di1.10.490.10, 2 hits
    3.40.50.80, 1 hit
    InterProiView protein in InterPro
    IPR008333 Cbr1-like_FAD-bd_dom
    IPR017927 FAD-bd_FR_type
    IPR039261 FNR_nucleotide-bd
    IPR000971 Globin
    IPR009050 Globin-like_sf
    IPR012292 Globin/Proto
    IPR023950 Hmp
    IPR001433 OxRdtase_FAD/NAD-bd
    IPR017938 Riboflavin_synthase-like_b-brl
    PANTHERiPTHR43396 PTHR43396, 1 hit
    PfamiView protein in Pfam
    PF00970 FAD_binding_6, 1 hit
    PF00175 NAD_binding_1, 1 hit
    SUPFAMiSSF46458 SSF46458, 1 hit
    SSF52343 SSF52343, 1 hit
    SSF63380 SSF63380, 1 hit
    PROSITEiView protein in PROSITE
    PS51384 FAD_FR, 1 hit
    PS01033 GLOBIN, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    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 nameiHMP_GIAIC
    <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: E2RTZ4
    Secondary accession number(s): A8BWC7, Q86QZ2
    <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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 31, 2011
    Last sequence update: November 30, 2010
    Last modified: May 8, 2019
    This is version 51 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)

    <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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
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