Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Aldehyde oxidase 2

Gene

AOX2

Organism
Cavia porcellus (Guinea pig)
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 bindingi47 – 471Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi52 – 521Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi55 – 551Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi77 – 771Iron-sulfur 1 (2Fe-2S)By similarity
Binding sitei116 – 1161MolybdopterinBy similarity
Metal bindingi117 – 1171Iron-sulfur 2 (2Fe-2S)By similarity
Metal bindingi120 – 1201Iron-sulfur 2 (2Fe-2S)By similarity
Metal bindingi152 – 1521Iron-sulfur 2 (2Fe-2S)By similarity
Metal bindingi154 – 1541Iron-sulfur 2 (2Fe-2S)By similarity
Binding sitei360 – 3601FADBy similarity
Binding sitei364 – 3641FADBy similarity
Binding sitei373 – 3731FADBy similarity
Binding sitei417 – 4171FAD; via amide nitrogenBy similarity
Binding sitei821 – 8211Molybdopterin; via amide nitrogenBy similarity
Binding sitei1062 – 10621Molybdopterin; via amide nitrogenBy similarity
Binding sitei1218 – 12181MolybdopterinBy similarity
Active sitei1287 – 12871Proton acceptor; for azaheterocycle hydroxylase activityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi270 – 2778FADBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

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

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
OrganismiCavia porcellus (Guinea pig)
Taxonomic identifieri10141 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia
Proteomesi
  • UP000005447 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13351335Aldehyde oxidase 2PRO_0000425243Add
BLAST

Expressioni

Tissue specificityi

Detected in kidney, Harderian gland and olfactory mucosa.1 Publication

Interactioni

Subunit structurei

Homodimer.By similarity

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 95882Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini242 – 427186FAD-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

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.
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.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

H9TB19-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPHPPGSDVL VFFVNGRKVT ERDVDPEVTL LTYLRRNLGL TGTKSACGGG
60 70 80 90 100
SCGTCTVMLS RFDLASRKPR HIAVTACLVP LCSLHGAAVT TVEGVGSIRT
110 120 130 140 150
RVHPVQERIA KSHGTQCGFC TPGMVMSLYA LLRSHPQPSE EQLLEALAGN
160 170 180 190 200
LCRCTGYRPI LESGRTFCLD SASCGQHGAR QCCLDQPGDG TCPPGRNGPQ
210 220 230 240 250
AHMCSELIPR TEFQPWDPTQ EPIFPPELMR MAESPVQPSL TFRGDRVTWV
260 270 280 290 300
SPGSLQELLA LRARHPEAPL VLGNTALGPA QRSQGRVHPL LISPARIPEL
310 320 330 340 350
STVTETSDGL TIGASCSLAQ LQDILAKSIS QLPVEKTQTL RALAKALRSV
360 370 380 390 400
AGLQVRNLAS LGGHVMSLHS YSDLNPILAV GQAALHLRSE GGARLISLDE
410 420 430 440 450
HFLAGVVSAS LQPGEILESV HIPHSQKWEF VFSFRQAQAP QNASPHVSAG
460 470 480 490 500
MRVRFTEGTD TIEDLSIAYG GVGTTTVMAP QACQRLLGRH WTEETLDEAC
510 520 530 540 550
RLVLGEVTIP GAAPGGRVEF RRTLLVSFLF RFYLQVLQEL KAHRFLKPPC
560 570 580 590 600
TPRTLSDTWK YPQLPDQTLG ALEDVPIMVP RGVQMYERVD PQQPPQDPVG
610 620 630 640 650
RSIMHLSGLK HATGEAVFCD DLPRVDKELF MALVTSTRPH AKIVSVDPAE
660 670 680 690 700
ALRLPGVVAI VTAEDIPGTN GTEDDKLLAV DKVLCVGQVI CAVVAETDVQ
710 720 730 740 750
ARQATGSVRV TYEDLEPVVL SIQDAIGHSS FLCPEKKLEL GNTEEAFEDV
760 770 780 790 800
DHILEGEVHV GGQEHFYMET QRVLVIPKVE DQELDIYAST QDPAHMQKTV
810 820 830 840 850
SSTLNVPLNR VTCHVKRVGG GFGGKQGRSA MLGAIAAVGA IKTGRPVRLV
860 870 880 890 900
LDRDEDMLIT GGRHPLFGKY KVGFMDSGRI KALDIQCYIN GGCVLDYSEL
910 920 930 940 950
VIEFLILKLE NAYKIRNLRF RGRACRTNLP SNTAFRGFGF PQGALVIESC
960 970 980 990 1000
ITAVAAKCGL LPEKVREKNM YRTVDKTIYK QAFSPEPLHR CWAECLEQAD
1010 1020 1030 1040 1050
VPGRRALADA FNRQSPWRKR GIAVVPMKFS VGFAATSYHQ AAALVHIYTD
1060 1070 1080 1090 1100
GSVLVTHGGN ELGQGIHTKM LQVASRELRV PLCRLHIQET STATVPNTVT
1110 1120 1130 1140 1150
TAASVGADVN GRAVQNACQT LLKRLEPIMK KNPEGTWEAW VEAAFEQRIS
1160 1170 1180 1190 1200
LSATGYFRGY KAFMDWEKGE GEPFPYCVFG AACSEVEIDC LTGAHRKLRT
1210 1220 1230 1240 1250
DIVMDAGCSL NPALDIGQVE GAFLQGAGLY TTEELHYSPE GALLSGGPEE
1260 1270 1280 1290 1300
YKIPTAADVP EKLNVTLLPS AQAQTGLTIY SSKGLGESGM FLGSSVFFAI
1310 1320 1330
QDAVAAARRD RGLAEDFTVP REDPGTCKPW SISVA
Length:1,335
Mass (Da):144,924
Last modified:February 19, 2014 - v2
Checksum:iCC916D8865BFC555
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti140 – 1401E → G in AFG18183 (PubMed:23263164).Curated
Sequence conflicti854 – 8541D → N in AFG18183 (PubMed:23263164).Curated
Sequence conflicti1074 – 10741A → V in AFG18183 (PubMed:23263164).Curated
Sequence conflicti1177 – 11771C → Y in AFG18183 (PubMed:23263164).Curated
Sequence conflicti1201 – 12011D → G in AFG18183 (PubMed:23263164).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JQ280311 mRNA. Translation: AFG18183.1.
AAKN02051282 Genomic DNA. No translation available.
AAKN02051283 Genomic DNA. No translation available.
RefSeqiNP_001265693.1. NM_001278764.1.

Genome annotation databases

GeneIDi100719938.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JQ280311 mRNA. Translation: AFG18183.1.
AAKN02051282 Genomic DNA. No translation available.
AAKN02051283 Genomic DNA. No translation available.
RefSeqiNP_001265693.1. NM_001278764.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100719938.

Organism-specific databases

CTDi213043.

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.
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.
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. "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: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, IDENTIFICATION OF PARALOGS.
  2. "A high-resolution map of human evolutionary constraint using 29 mammals."
    Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.
    , Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.
    Nature 478:476-482(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 2N.

Entry informationi

Entry nameiAOXB_CAVPO
AccessioniPrimary (citable) accession number: H9TB19
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 19, 2014
Last sequence update: February 19, 2014
Last modified: May 11, 2016
This is version 20 of the entry and version 2 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.