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Protein

Aldehyde oxidase 2

Gene

Aox2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as phthalazine, as well as aldehydes, such as benzaldehyde and retinal.By similarity

Catalytic activityi

An aldehyde + H2O + O2 = a carboxylate + H2O2.

Cofactori

Protein has several cofactor binding sites:
  • [2Fe-2S] clusterBy similarityNote: Binds 2 [2Fe-2S] clusters per subunit.By similarity
  • FADBy similarityNote: Binds 1 FAD per subunit.By similarity
  • Mo-molybdopterinBy similarityNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi48 – 481Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi53 – 531Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi56 – 561Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi78 – 781Iron-sulfur 1 (2Fe-2S)By similarity
Binding sitei117 – 1171MolybdopterinBy similarity
Metal bindingi118 – 1181Iron-sulfur 2 (2Fe-2S)By similarity
Metal bindingi121 – 1211Iron-sulfur 2 (2Fe-2S)By similarity
Metal bindingi153 – 1531Iron-sulfur 2 (2Fe-2S)By similarity
Metal bindingi155 – 1551Iron-sulfur 2 (2Fe-2S)By similarity
Binding sitei356 – 3561FADBy similarity
Binding sitei360 – 3601FADBy similarity
Binding sitei369 – 3691FADBy similarity
Binding sitei413 – 4131FAD; via amide nitrogenBy similarity
Binding sitei812 – 8121Molybdopterin; via amide nitrogenBy similarity
Binding sitei1053 – 10531Molybdopterin; via amide nitrogenBy similarity
Binding sitei1209 – 12091MolybdopterinBy similarity
Active sitei1276 – 12761Proton acceptor; for azaheterocycle hydroxylase activityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi266 – 2738FADBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum

Enzyme and pathway databases

BRENDAi1.2.3.1. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde oxidase 2 (EC:1.2.3.1)
Alternative name(s):
Aldehyde oxidase homolog 3
Azaheterocycle hydroxylase 2 (EC:1.17.3.-)
Gene namesi
Name:Aox2
Synonyms:Aoh3, Aox3l1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1359668. Aox2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13451345Aldehyde oxidase 2PRO_0000425246Add
BLAST

Proteomic databases

PaxDbiQ5QE78.
PRIDEiQ5QE78.

PTM databases

iPTMnetiQ5QE78.
PhosphoSiteiQ5QE78.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000047535.

Structurei

3D structure databases

ProteinModelPortaliQ5QE78.
SMRiQ5QE78. Positions 7-168.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 96882Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini238 – 423186FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the xanthine dehydrogenase family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0430. Eukaryota.
COG4630. LUCA.
COG4631. LUCA.
HOGENOMiHOG000191197.
HOVERGENiHBG004182.
KOiK00157.
OrthoDBiEOG7QRQSZ.
PhylomeDBiQ5QE78.

Family and domain databases

Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.1170.50. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR014313. Aldehyde_oxidase.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
[Graphical view]
PfamiPF01315. 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.
[Graphical view]
PIRSFiPIRSF000127. Xanthine_DH. 1 hit.
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsiTIGR02969. mam_aldehyde_ox. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5QE78-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPCPSQSSDE LEFFVNGKKV TEKNVDPEVT LLAFLRKNLR LTGTKYACGT
60 70 80 90 100
GSCGACTVMV SQHDPVCKKT RHFSVMACLV PLCSLHGAAV TTVEGVGSIK
110 120 130 140 150
TRLHPVQERL AKSHGTQCGF CSPGMVMSMY ALLRNHPQPS EEQLLEALGG
160 170 180 190 200
NLCRCTGYRP ILESGRTFCM ESDGCLQKGT GQCCLDQKEG DSSGSKSDIC
210 220 230 240 250
TELFVKDEFQ PLDPTQELIF PPELLRMAEN PEKQTLTFYG ERITWIAPGT
260 270 280 290 300
LQELLVLKAK YPEAPLISGN TALGPAMKSQ GHFYPVLLSP ARIPDLRMVT
310 320 330 340 350
KTSGGLTIGA CCSLAQVKDV LAESISELPE EKTQTYRALL KHLRSLAGQQ
360 370 380 390 400
IRNMASLGGH VISRHYYSDL NPILSVGNAT LNLLSEEGLR QIPLNGHFLA
410 420 430 440 450
GLANEDLKPE EILGSVYIPH SQKREFVSAF RQAQCHQNAL PDVNAGMRVL
460 470 480 490 500
FKEGTDIIEE LSIAYGGVGP TTVSAHRSCQ QLLGRRWNAL LLDEACRLLL
510 520 530 540 550
DEVSLPGSAV GGKVEFRRTL IVSFFFKFYL EVLQELKADK RLLPESTDSQ
560 570 580 590 600
RYPEIADGSR SSLGDFQVTL PQGVQTYQRV NSHQPLQDPV GRPIMHLSGL
610 620 630 640 650
KHATGEAVFC DDIPRVDKEL FMALVTSTRA HARIISIDSS EVLDLPGVVD
660 670 680 690 700
VITAEDIPGN NGEEDDKLLA VDKVLCVGQV VCAVVAETDV QAKRATKKIK
710 720 730 740 750
ITYEDLKPVL FTIEDAIQHN SFLCPEKKLE QGNMEEAFEN VDQIVEGKVH
760 770 780 790 800
VGGQEHFYME TQRVLVIPKT EDKELDMYVS TQDPAHVQKT VSSALNIPLS
810 820 830 840 850
RITCHVKRVG GGFGGKVGRP AVFGAIAAVG AVKTGRPIRL VLDREDDMLI
860 870 880 890 900
TGGRHPLFAK YKVGFMNSGR IKALDIECYI NGGCTLDDSE LVTEFLVLKL
910 920 930 940 950
ENAYKIRNLR LRGRACMTNL PSNTAFRGFG FPQGALVTES CITAVAAKCG
960 970 980 990 1000
LPPEKIREKN MYKTVDKTIY KQAFNPEPLI RCWNECLDKS SFAIRRTRVD
1010 1020 1030 1040 1050
EFNKKSYWRK RGIAVVPMKF SVGFAATSYH QAAALVHIYT DGSVLVAHGG
1060 1070 1080 1090 1100
NELGQGIHTK MLQVASRELK IPMSYLHTSE TCTAAVPNTI ATAASVGADV
1110 1120 1130 1140 1150
NGRAVQNACQ ILLKRLEPVI KKNPEGTWRD WIEAAFEQRI SLSATGYNRG
1160 1170 1180 1190 1200
YKAFMDWEKG EGDPFPYYVY GAACSEVEID CLTGAHKKMR TDIVMDACCS
1210 1220 1230 1240 1250
LNPAIDVGQI EGAFIQGMGL YTTEDVHYSP EGVLYSRSPD KYKIPTVTDV
1260 1270 1280 1290 1300
PEQFNVSLLP SSQTPLTIYS SKGLGESGMF LGSSVFFAIA DAVAAARRQR
1310 1320 1330 1340
DIAEDFTVKS PATPERVRMA CADRFTDMIP RDDPKTFKPW SIPIA
Length:1,345
Mass (Da):147,872
Last modified:January 4, 2005 - v1
Checksum:i697802975A12B03C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti70 – 701T → TK in AABR06060563 (PubMed:15057822).Curated
Sequence conflicti70 – 701T → TK in AABR06060564 (PubMed:15057822).Curated
Sequence conflicti70 – 701T → TK in AABR06060565 (PubMed:15057822).Curated
Sequence conflicti70 – 701T → TK in AABR06060566 (PubMed:15057822).Curated
Sequence conflicti356 – 38631SLGGH…NLLSE → VVSGHIVVSHHCQPLKACLS LSCIEMAFPST in AABR06060563 (PubMed:15057822).CuratedAdd
BLAST
Sequence conflicti356 – 38631SLGGH…NLLSE → VVSGHIVVSHHCQPLKACLS LSCIEMAFPST in AABR06060564 (PubMed:15057822).CuratedAdd
BLAST
Sequence conflicti356 – 38631SLGGH…NLLSE → VVSGHIVVSHHCQPLKACLS LSCIEMAFPST in AABR06060565 (PubMed:15057822).CuratedAdd
BLAST
Sequence conflicti356 – 38631SLGGH…NLLSE → VVSGHIVVSHHCQPLKACLS LSCIEMAFPST in AABR06060566 (PubMed:15057822).CuratedAdd
BLAST
Sequence conflicti1148 – 11481N → F in AABR06060563 (PubMed:15057822).Curated
Sequence conflicti1148 – 11481N → F in AABR06060564 (PubMed:15057822).Curated
Sequence conflicti1148 – 11481N → F in AABR06060565 (PubMed:15057822).Curated
Sequence conflicti1148 – 11481N → F in AABR06060566 (PubMed:15057822).Curated
Sequence conflicti1225 – 12262DV → EL in AABR06060563 (PubMed:15057822).Curated
Sequence conflicti1225 – 12262DV → EL in AABR06060564 (PubMed:15057822).Curated
Sequence conflicti1225 – 12262DV → EL in AABR06060565 (PubMed:15057822).Curated
Sequence conflicti1225 – 12262DV → EL in AABR06060566 (PubMed:15057822).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY665588 mRNA. Translation: AAV68255.1.
AABR06060563 Genomic DNA. No translation available.
AABR06060564 Genomic DNA. No translation available.
AABR06060565 Genomic DNA. No translation available.
AABR06060566 Genomic DNA. No translation available.
RefSeqiNP_001008522.1. NM_001008522.1.
UniGeneiRn.215801.

Genome annotation databases

GeneIDi316421.
KEGGirno:316421.
UCSCiRGD:1359668. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY665588 mRNA. Translation: AAV68255.1.
AABR06060563 Genomic DNA. No translation available.
AABR06060564 Genomic DNA. No translation available.
AABR06060565 Genomic DNA. No translation available.
AABR06060566 Genomic DNA. No translation available.
RefSeqiNP_001008522.1. NM_001008522.1.
UniGeneiRn.215801.

3D structure databases

ProteinModelPortaliQ5QE78.
SMRiQ5QE78. Positions 7-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000047535.

PTM databases

iPTMnetiQ5QE78.
PhosphoSiteiQ5QE78.

Proteomic databases

PaxDbiQ5QE78.
PRIDEiQ5QE78.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi316421.
KEGGirno:316421.
UCSCiRGD:1359668. rat.

Organism-specific databases

CTDi213043.
RGDi1359668. Aox2.

Phylogenomic databases

eggNOGiKOG0430. Eukaryota.
COG4630. LUCA.
COG4631. LUCA.
HOGENOMiHOG000191197.
HOVERGENiHBG004182.
KOiK00157.
OrthoDBiEOG7QRQSZ.
PhylomeDBiQ5QE78.

Enzyme and pathway databases

BRENDAi1.2.3.1. 5301.

Miscellaneous databases

PROiQ5QE78.

Family and domain databases

Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.1170.50. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR014313. Aldehyde_oxidase.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
[Graphical view]
PfamiPF01315. 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.
[Graphical view]
PIRSFiPIRSF000127. Xanthine_DH. 1 hit.
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsiTIGR02969. mam_aldehyde_ox. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The aldehyde oxidase gene cluster in mice and rats. Aldehyde oxidase homologue 3, a novel member of the molybdo-flavoenzyme family with selective expression in the olfactory mucosa."
    Kurosaki M., Terao M., Barzago M.M., Bastone A., Bernardinello D., Salmona M., Garattini E.
    J. Biol. Chem. 279:50482-50498(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: CD Charles River.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. "Structure and evolution of vertebrate aldehyde oxidases: from gene duplication to gene suppression."
    Kurosaki M., Bolis M., Fratelli M., Barzago M.M., Pattini L., Perretta G., Terao M., Garattini E.
    Cell. Mol. Life Sci. 70:1807-1830(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PARALOGS.

Entry informationi

Entry nameiAOXB_RAT
AccessioniPrimary (citable) accession number: Q5QE78
Secondary accession number(s): D4A6S5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 19, 2014
Last sequence update: January 4, 2005
Last modified: June 8, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:23263164).1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.