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Entry version 127 (11 Dec 2019)
Sequence version 1 (01 Jan 1998)
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Protein

Indole-3-acetaldehyde oxidase

Gene

AO1

Organism
Zea mays (Maize)
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

In higher plants aldehyde oxidases (AO) appear to be homo- and heterodimeric assemblies of AO subunits with probably different physiological functions. Involved in the biosynthesis of auxin from (indol-3-yl)acetaldehyde. Can also use indole-3-aldehyde and benzaldehyde as substrate.1 Publication

<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 <a href="http://www.uniprot.org/help/function_section">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

Inhibited by 2-mercaptoethanol, p-chloromercuribenzoate, and iodoacetate.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

  1. KM=3.2 µM for (indol-3-yl)acetaldehyde (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor)1 Publication
  2. KM=4.5 µM for indol-3-aldehyde (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor)1 Publication
  3. KM=1.5 µM for benzaldehyde (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor)1 Publication
  4. KM=2.9 µM for protocatechualdehyde (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor)1 Publication
  5. KM=5 µM for (indol-3-yl)acetaldehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)1 Publication
  6. KM=14 µM for indol-3-aldehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)1 Publication
  7. KM=5 µM for benzaldehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)1 Publication
  8. KM=26 µM for protocatechualdehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)1 Publication
  9. KM=250 µM for phenylacetaldehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)1 Publication
  10. KM=26 µM for butyraldehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)1 Publication
  11. KM=74 µM for propionaldehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)1 Publication
  12. KM=345 µM for acetaldehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)1 Publication
  1. Vmax=76 nmol/min/mg enzyme with (indol-3-yl)acetaldehyde as substrate (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor)1 Publication
  2. Vmax=69 nmol/min/mg enzyme with indol-3-aldehyde as substrate (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor)1 Publication
  3. Vmax=453 nmol/min/mg enzyme with benzaldehyde as substrate (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor)1 Publication
  4. Vmax=175 nmol/min/mg enzyme with protocatechualdehyde as substrate (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor)1 Publication
  5. Vmax=28 nmol/min/mg enzyme with (indol-3-yl)acetaldehyde as substrate (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)1 Publication
  6. Vmax=190 nmol/min/mg enzyme with indol-3-aldehyde as substrate (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)1 Publication
  7. Vmax=247 nmol/min/mg enzyme with benzaldehyde as substrate (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)1 Publication
  8. Vmax=316 nmol/min/mg enzyme with protocatechualdehyde as substrate (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)1 Publication
  9. Vmax=120 nmol/min/mg enzyme with phenylacetaldehyde as substrate (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)1 Publication
  10. Vmax=113 nmol/min/mg enzyme with butyraldehyde as substrate (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)1 Publication
  11. Vmax=70 nmol/min/mg enzyme with propionaldehyde as substrate (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)1 Publication
  12. Vmax=57 nmol/min/mg enzyme with acetaldehyde as substrate (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)1 Publication

pH dependencei

Optimum pH is 7-8.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bindingi50Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
Metal bindingi55Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
Metal bindingi58Iron-sulfur (2Fe-2S)PROSITE-ProRule 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
Biological processAbscisic acid biosynthesis, Auxin biosynthesis
Ligand2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.2.3.1 6752

<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:
Indole-3-acetaldehyde oxidase (EC:1.2.3.7)
Short name:
IAA oxidase
Alternative name(s):
Aldehyde oxidase
Short name:
ZmAO-1
<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:AO1
<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>OrganismiZea mays (Maize)
<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 identifieri4577 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogonodaeAndropogoneaeTripsacinaeZea
<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
  • UP000007305 <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: Unplaced

Organism-specific databases

Maize Genetics and Genomics Database

More...
MaizeGDBi
275805

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

<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_00004188421 – 1358Indole-3-acetaldehyde oxidaseAdd BLAST1358

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
O23887

<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 provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Mostly expressed in roots, and, to a lower extent, in mesocotyl, leaves and coleoptile. Accumulates in apical region of maize coleoptiles (at protein level).1 Publication

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
O23887 baseline and differential

<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

Aldehyde oxidases (AO) are homodimers and heterodimers of AO subunits.

By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
4577.GRMZM2G141535_P01

<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
O23887

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_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>Domaini11 – 982Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST88
Domaini241 – 419FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST179

<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 xanthine dehydrogenase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0430 Eukaryota
COG4630 LUCA
COG4631 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000191197

KEGG Orthology (KO)

More...
KOi
K11817

Database of Orthologous Groups

More...
OrthoDBi
48717at2759

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002888 2Fe-2S-bd
IPR036884 2Fe-2S-bd_dom_sf
IPR036010 2Fe-2S_ferredoxin-like_sf
IPR001041 2Fe-2S_ferredoxin-type
IPR006058 2Fe2S_fd_BS
IPR000674 Ald_Oxase/Xan_DH_a/b
IPR036856 Ald_Oxase/Xan_DH_a/b_sf
IPR016208 Ald_Oxase/xanthine_DH
IPR008274 AldOxase/xan_DH_Mopterin-bd
IPR037165 AldOxase/xan_DH_Mopterin-bd_sf
IPR005107 CO_DH_flav_C
IPR036683 CO_DH_flav_C_dom_sf
IPR016166 FAD-bd_PCMH
IPR036318 FAD-bd_PCMH-like_sf
IPR002346 Mopterin_DH_FAD-bd

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01315 Ald_Xan_dh_C, 1 hit
PF02738 Ald_Xan_dh_C2, 1 hit
PF03450 CO_deh_flav_C, 1 hit
PF00941 FAD_binding_5, 1 hit
PF00111 Fer2, 1 hit
PF01799 Fer2_2, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000127 Xanthine_DH, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01008 Ald_Xan_dh_C, 1 hit
SM01092 CO_deh_flav_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47741 SSF47741, 1 hit
SSF54292 SSF54292, 1 hit
SSF54665 SSF54665, 1 hit
SSF55447 SSF55447, 1 hit
SSF56003 SSF56003, 1 hit
SSF56176 SSF56176, 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
PS51387 FAD_PCMH, 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.

O23887-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGKEAGAAES STVVLAVNGK RYEAAGVAPS TSLLEFLRTQ TPVRGPKLGC
60 70 80 90 100
GEGGCGACVV LVSKYDPATD EVTEFSASSC LTLLHSVDRC SVTTSEGIGN
110 120 130 140 150
TRDGYHPVQQ RLSGFHASQC GFCTPGMCMS IFSALVKADN KSDRPDPPAG
160 170 180 190 200
FSKITTSEAE KAVSGNLCRC TGYRPIVDTC KSFASDVDLE DLGLNCFWKK
210 220 230 240 250
GEEPAEVSRL PGYNSGAVCT FPEFLKSEIK STMKQVNDVP IAASGDGWYH
260 270 280 290 300
PKSIEELHRL FDSSWFDDSS VKIVASNTGS GVYKDQDLYD KYIDIKGIPE
310 320 330 340 350
LSVINKNDKA IELGSVVSIS KAIEVLSDGN LVFRKIADHL NKVASPFVRN
360 370 380 390 400
TATIGGNIMM AQRLPFESDV ATVLLAAGST VTVQVASKRL CFTLEEFLEQ
410 420 430 440 450
PPCDSRTLLL SIFIPEWGSD YVTFETFRAA PRPFGNAVSY VNSAFLARTS
460 470 480 490 500
GSLLIEDICL AFGAYGVDHA IRAKKVEDFL KGKSLSSFVI LEAIKLLKDT
510 520 530 540 550
VSPSEGTTHH EYRVSLAVSF LFSFLSSLAN SSSAPSNIDT PNGSYTHETG
560 570 580 590 600
SNVDSPERHI KVDSNDLPIR SRQEMVFSDE YKPVGKPIKK VGAEIQASGE
610 620 630 640 650
AVYVDDIPAP KDCLYGAFIY STHPHAHVRS INFKSSLASQ KVITVITAKD
660 670 680 690 700
IPSGGENIGS SFLMQGEALF ADPIAEFAGQ NIGVVIAETQ RYANMAAKQA
710 720 730 740 750
VVEYSTENLQ PPILTIEDAI QRNSYIQIPP FLAPKPVGDY NKGMAEADHK
760 770 780 790 800
ILSAEVKLES QYYFYMETQA ALAIPDEDNC ITIYSSTQMP ELTQNLIARC
810 820 830 840 850
LGIPFHNVRV ISRRVGGGFG GKAMKATHTA CACALAAFKL RRPVRMYLDR
860 870 880 890 900
KTDMIMAGGR HPMKAKYSVG FKSDGKITAL HLDLGINAGI SPDVSPLMPR
910 920 930 940 950
AIIGALKKYN WGTLEFDTKV CKTNVSSKSA MRAPGDVQGS FIAEAIIEHV
960 970 980 990 1000
ASALALDTNT VRRKNLHDFE SLEVFYGESA GEASTYSLVS MFDKLALSPE
1010 1020 1030 1040 1050
YQHRAAMIEQ FNSSNKWKKR GISCVPATYE VNLRPTPGKV SIMNDGSIAV
1060 1070 1080 1090 1100
EVGGIEIGQG LWTKVKQMTA FGLGQLCPDG GECLLDKVRV IQADTLSLIQ
1110 1120 1130 1140 1150
GGMTAGSTTS ETSCETVRQS CVALVEKLNP IKESLEAKSN TVEWSALIAQ
1160 1170 1180 1190 1200
ASMASVNLSA QPYWTPDPSF KSYLNYGAGT SEVEVDILTG ATTILRSDLV
1210 1220 1230 1240 1250
YDCGQSLNPA VDLGQIEGCF VQGIGFFTNE DYKTNSDGLV IHDGTWTYKI
1260 1270 1280 1290 1300
PTVDNIPKEF NVEMFNSAPD KKRVLSSKAS GEPPLVLATS VHCAMREAIR
1310 1320 1330 1340 1350
AARKEFSVST SPAKSAVTFQ MDVPATMPVV KELCGLDVVE RYLENVSAAS

AGPNTAKA
Length:1,358
Mass (Da):146,683
Last modified:January 1, 1998 - 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:i82449227AFB14861
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence ACN28172 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti1116T → A in ACN28172 (PubMed:19936069).Curated1
Sequence conflicti1127 – 1129KLN → RLK in ACN28172 (PubMed:19936069).Curated3
Sequence conflicti1162P → A in ACN28172 (PubMed:19936069).Curated1
Sequence conflicti1289T → A in ACN28172 (PubMed:19936069).Curated1

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
D88451 mRNA Translation: BAA23226.1
BT063475 mRNA Translation: ACN28172.1 Different initiation.

Protein sequence database of the Protein Information Resource

More...
PIRi
T01698

NCBI Reference Sequences

More...
RefSeqi
NP_001105308.1, NM_001111838.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
542228

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
zma:542228

<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
D88451 mRNA Translation: BAA23226.1
BT063475 mRNA Translation: ACN28172.1 Different initiation.
PIRiT01698
RefSeqiNP_001105308.1, NM_001111838.1

3D structure databases

SMRiO23887
ModBaseiSearch...

Protein-protein interaction databases

STRINGi4577.GRMZM2G141535_P01

Proteomic databases

PaxDbiO23887

Genome annotation databases

GeneIDi542228
KEGGizma:542228

Organism-specific databases

MaizeGDBi275805

Phylogenomic databases

eggNOGiKOG0430 Eukaryota
COG4630 LUCA
COG4631 LUCA
HOGENOMiHOG000191197
KOiK11817
OrthoDBi48717at2759

Enzyme and pathway databases

BRENDAi1.2.3.1 6752

Gene expression databases

ExpressionAtlasiO23887 baseline and differential

Family and domain databases

InterProiView protein in InterPro
IPR002888 2Fe-2S-bd
IPR036884 2Fe-2S-bd_dom_sf
IPR036010 2Fe-2S_ferredoxin-like_sf
IPR001041 2Fe-2S_ferredoxin-type
IPR006058 2Fe2S_fd_BS
IPR000674 Ald_Oxase/Xan_DH_a/b
IPR036856 Ald_Oxase/Xan_DH_a/b_sf
IPR016208 Ald_Oxase/xanthine_DH
IPR008274 AldOxase/xan_DH_Mopterin-bd
IPR037165 AldOxase/xan_DH_Mopterin-bd_sf
IPR005107 CO_DH_flav_C
IPR036683 CO_DH_flav_C_dom_sf
IPR016166 FAD-bd_PCMH
IPR036318 FAD-bd_PCMH-like_sf
IPR002346 Mopterin_DH_FAD-bd
PfamiView protein in Pfam
PF01315 Ald_Xan_dh_C, 1 hit
PF02738 Ald_Xan_dh_C2, 1 hit
PF03450 CO_deh_flav_C, 1 hit
PF00941 FAD_binding_5, 1 hit
PF00111 Fer2, 1 hit
PF01799 Fer2_2, 1 hit
PIRSFiPIRSF000127 Xanthine_DH, 1 hit
SMARTiView protein in SMART
SM01008 Ald_Xan_dh_C, 1 hit
SM01092 CO_deh_flav_C, 1 hit
SUPFAMiSSF47741 SSF47741, 1 hit
SSF54292 SSF54292, 1 hit
SSF54665 SSF54665, 1 hit
SSF55447 SSF55447, 1 hit
SSF56003 SSF56003, 1 hit
SSF56176 SSF56176, 1 hit
PROSITEiView protein in PROSITE
PS00197 2FE2S_FER_1, 1 hit
PS51085 2FE2S_FER_2, 1 hit
PS51387 FAD_PCMH, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiALDO1_MAIZE
<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: O23887
Secondary accession number(s): C0P5A6
<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: September 5, 2012
Last sequence update: January 1, 1998
Last modified: December 11, 2019
This is version 127 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 programPlant 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

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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