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UniProtKB - Q06278 (AOXA_HUMAN)

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Protein

Aldehyde oxidase

Gene

AOX1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis.9 Publications

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:22335465).1 Publication

Caution

Was originally thought to be a xanthine dehydrogenase.1 Publication

Catalytic activityi

An aldehyde + H2O + O2 = a carboxylate + H2O2.2 Publications
Retinal + O2 + H2O = retinoate + H2O2.By similarity

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Is very potently inhibited by raloxifene (PubMed:26842593). Also inhibited by estradiol, ethinyl estradiol, hydralazine, menadione, isovanillin and thioridazine. Not inhibited by allopurinol, a xanthine dehydrogenase potent inhibitor (PubMed:22031625, PubMed:22522748, PubMed:22996261, PubMed:9224775, PubMed:26322824).6 Publications

Kineticsi

kcat is 6.4 min(-1) for benzaldehyde oxidation, 5.6 min(-1) for phthalazine oxidation, 12.2 min(-1) for phenanthridine oxidation and 5.6 min(-1) for chloroquinazolinone oxidation.1 Publication
  1. KM=4.6 µM for benzaldehyde (in the presence of 2,6-dichlorophenol indophenol as electron acceptor)1 Publication
  2. KM=45.18 µM for benzaldehyde (in the presence of ferricyanide as electron acceptor)1 Publication
  3. KM=1.3 µM for phthalazine (at 25 degrees Celsius and pH 7.5)1 Publication
  4. KM=8.96 µM for phthalazine (in the presence of 2,6-dichlorophenol indophenol as electron acceptor)1 Publication
  5. KM=125.7 µM for phthalazine (in the presence of ferricyanide as electron acceptor)1 Publication
  6. KM=0.78 µM for phenanthridine (in the pres 2,6-dichlorophenol indophenol as electron acceptor)1 Publication
  7. KM=25.5 µM for phenanthridine (in the presence of ferricyanide as electron acceptor)1 Publication
  8. KM=26.53 µM for phenanthridine (in the presence of molecular oxygen as electron acceptor)1 Publication
  9. KM=3.9 µM for phenanthridine (at 25 degrees Celsius and pH 7.5)1 Publication
  10. KM=5.2 µM for chloroquinazolinone (at 25 degrees Celsius and pH 7.5)1 Publication
  11. KM=0.42 mM for 6-deoxypenciclovir (at 37 degrees Celsius and pH 7)1 Publication
  12. KM=0.15 mM for famciclovir (at 37 degrees Celsius and pH 7)1 Publication
  13. KM=6.3 µM for N-[(2-dimethylamino)ethyl]acridine-4-carboxamide (at 37 degrees Celsius and pH 7.4)1 Publication
  1. Vmax=16 nmol/min/mg enzyme with 6-deoxypenciclovir as substrate1 Publication
  2. Vmax=61 nmol/min/mg enzyme with famciclovir as substrate1 Publication
  3. Vmax=2.3 nmol/min/mg enzyme with N-[(2-dimethylamino)ethyl]acridine-4-carboxamide as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi44Iron-sulfur 1 (2Fe-2S)Combined sources1 Publication1
Metal bindingi49Iron-sulfur 1 (2Fe-2S)Combined sources2 Publications1
Metal bindingi52Iron-sulfur 1 (2Fe-2S)Combined sources2 Publications1
Metal bindingi74Iron-sulfur 1 (2Fe-2S)Combined sources2 Publications1
Binding sitei113MolybdopterinCombined sources1 Publication1
Metal bindingi114Iron-sulfur 2 (2Fe-2S)Combined sources2 Publications1
Metal bindingi117Iron-sulfur 2 (2Fe-2S)Combined sources2 Publications1
Metal bindingi149Iron-sulfur 2 (2Fe-2S)Combined sources2 Publications1
Metal bindingi151Iron-sulfur 2 (2Fe-2S)Combined sources2 Publications1
Binding sitei151MolybdopterinCombined sources2 Publications1
Binding sitei345FAD; via amide nitrogenCombined sources1 Publication1
Binding sitei354FADCombined sources2 Publications1
Binding sitei358FADCombined sources2 Publications1
Binding sitei367FADCombined sources2 Publications1
Binding sitei411FAD; via amide nitrogen and carbonyl oxygenCombined sources2 Publications1
Binding sitei1047Molybdopterin; via carbonyl oxygenCombined sources2 Publications1
Binding sitei1203MolybdopterinCombined sources2 Publications1
Binding sitei1268Molybdopterin; via carbonyl oxygenCombined sources1 Publication1
Active sitei1270Proton acceptor; for azaheterocycle hydroxylase activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi264 – 271FADCombined sources2 Publications8

GO - Molecular functioni

  • 2 iron, 2 sulfur cluster binding Source: UniProtKB
  • aldehyde oxidase activity Source: UniProtKB
  • electron transfer activity Source: InterPro
  • flavin adenine dinucleotide binding Source: UniProtKB
  • geranial:oxygen oxidoreductase activity Source: UniProtKB-EC
  • heptaldehyde:oxygen oxidoreductase activity Source: UniProtKB-EC
  • identical protein binding Source: IntAct
  • iron ion binding Source: UniProtKB
  • molybdopterin cofactor binding Source: UniProtKB
  • NAD binding Source: InterPro
  • oxidoreductase activity, acting on CH-OH group of donors Source: InterPro
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors Source: GO_Central
  • protein homodimerization activity Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • drug metabolic process Source: UniProtKB
  • oxidation-reduction process Source: UniProtKB
  • vitamin B6 metabolic process Source: Reactome
  • xanthine catabolic process Source: GO_Central
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionOxidoreductase
Ligand2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000138356-MONOMER
BRENDAi1.2.3.1 2681
ReactomeiR-HSA-964975 Vitamins B6 activation to pyridoxal phosphate
SABIO-RKiQ06278

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde oxidaseImported (EC:1.2.3.12 Publications)
Alternative name(s):
Aldehyde oxidase 1
Azaheterocycle hydroxylase2 Publications (EC:1.17.3.-2 Publications)
Gene namesi
Name:AOX1Imported
Synonyms:AO
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000138356.13
HGNCiHGNC:553 AOX1
MIMi602841 gene
neXtProtiNX_Q06278

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi44C → W: Disrupts protein stability. 1 Publication1
Mutagenesisi1269G → R: No effect on dimerization. Loss of oxidase activity. 1 Publication1

Organism-specific databases

DisGeNETi316
OpenTargetsiENSG00000138356
PharmGKBiPA24842

Chemistry databases

ChEMBLiCHEMBL3257
DrugBankiDB00437 Allopurinol
DB00513 Aminocaproic Acid
DB00484 Brimonidine
DB03516 Eniluracil
DB04827 Ethyl carbamate
DB00426 Famciclovir
DB09054 Idelalisib
DB09078 Lenvatinib
DB00170 Menadione
DB01033 Mercaptopurine
DB00563 Methotrexate
DB00157 NADH
DB00339 Pyrazinamide
DB00481 Raloxifene
DB00962 Zaleplon
DB00909 Zonisamide

Polymorphism and mutation databases

BioMutaiAOX1
DMDMi215273968

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001661041 – 1338Aldehyde oxidaseAdd BLAST1338

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1068PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ06278
MaxQBiQ06278
PaxDbiQ06278
PeptideAtlasiQ06278
PRIDEiQ06278
ProteomicsDBi58430

PTM databases

iPTMnetiQ06278
PhosphoSitePlusiQ06278

Expressioni

Tissue specificityi

Abundant in liver, expressed in adipose tissue and at lower levels in lung, skeletal muscle, pancreas. In contrast to mice, no significant gender difference in AOX1 expression level (at protein level).7 Publications

Developmental stagei

Not detected in preadipocytes but strongly induced in mature adipocytes.1 Publication

Inductioni

In liver, is down-regulated by adiponectin and by the PPARA agonist, fenofibric acid.1 Publication

Gene expression databases

BgeeiENSG00000138356
CleanExiHS_AOX1
ExpressionAtlasiQ06278 baseline and differential
GenevisibleiQ06278 HS

Organism-specific databases

HPAiHPA040199
HPA040215

Interactioni

Subunit structurei

Homodimer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-3926368,EBI-3926368

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: UniProtKB
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi106813, 7 interactors
DIPiDIP-61698N
IntActiQ06278, 4 interactors
STRINGi9606.ENSP00000363832

Chemistry databases

BindingDBiQ06278

Structurei

Secondary structure

11338
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 11Combined sources6
Beta strandi14 – 20Combined sources7
Helixi27 – 33Combined sources7
Beta strandi45 – 49Combined sources5
Beta strandi53 – 60Combined sources8
Turni61 – 64Combined sources4
Beta strandi65 – 72Combined sources8
Helixi73 – 75Combined sources3
Helixi78 – 81Combined sources4
Beta strandi85 – 87Combined sources3
Helixi89 – 92Combined sources4
Beta strandi95 – 97Combined sources3
Helixi101 – 108Combined sources8
Helixi118 – 131Combined sources14
Helixi137 – 143Combined sources7
Helixi144 – 146Combined sources3
Beta strandi150 – 152Combined sources3
Helixi155 – 162Combined sources8
Helixi204 – 206Combined sources3
Helixi212 – 214Combined sources3
Helixi220 – 226Combined sources7
Beta strandi234 – 237Combined sources4
Beta strandi242 – 245Combined sources4
Helixi249 – 258Combined sources10
Helixi271 – 277Combined sources7
Beta strandi283 – 286Combined sources4
Helixi292 – 295Combined sources4
Beta strandi297 – 299Combined sources3
Beta strandi301 – 307Combined sources7
Helixi312 – 325Combined sources14
Turni328 – 330Combined sources3
Helixi332 – 343Combined sources12
Helixi347 – 352Combined sources6
Helixi355 – 361Combined sources7
Helixi369 – 374Combined sources6
Beta strandi378 – 382Combined sources5
Beta strandi387 – 391Combined sources5
Helixi394 – 397Combined sources4
Turni401 – 403Combined sources3
Beta strandi410 – 417Combined sources8
Beta strandi423 – 430Combined sources8
Beta strandi432 – 437Combined sources6
Beta strandi440 – 448Combined sources9
Beta strandi451 – 453Combined sources3
Beta strandi458 – 469Combined sources12
Helixi474 – 480Combined sources7
Helixi487 – 498Combined sources12
Helixi512 – 537Combined sources26
Turni539 – 541Combined sources3
Turni547 – 549Combined sources3
Helixi550 – 552Combined sources3
Beta strandi562 – 566Combined sources5
Beta strandi572 – 574Combined sources3
Helixi589 – 593Combined sources5
Helixi600 – 602Combined sources3
Beta strandi610 – 616Combined sources7
Beta strandi620 – 628Combined sources9
Helixi630 – 633Combined sources4
Beta strandi638 – 642Combined sources5
Helixi644 – 646Combined sources3
Helixi648 – 650Combined sources3
Beta strandi666 – 668Combined sources3
Beta strandi674 – 682Combined sources9
Helixi683 – 690Combined sources8
Beta strandi694 – 699Combined sources6
Helixi709 – 711Combined sources3
Beta strandi721 – 726Combined sources6
Helixi728 – 731Combined sources4
Helixi732 – 734Combined sources3
Beta strandi736 – 745Combined sources10
Beta strandi756 – 762Combined sources7
Beta strandi769 – 773Combined sources5
Helixi778 – 789Combined sources12
Helixi793 – 795Combined sources3
Beta strandi796 – 801Combined sources6
Helixi812 – 828Combined sources17
Beta strandi832 – 835Combined sources4
Helixi838 – 844Combined sources7
Beta strandi851 – 859Combined sources9
Beta strandi865 – 878Combined sources14
Helixi884 – 893Combined sources10
Turni894 – 897Combined sources4
Beta strandi901 – 911Combined sources11
Turni921 – 924Combined sources4
Helixi925 – 943Combined sources19
Helixi947 – 954Combined sources8
Beta strandi958 – 961Combined sources4
Beta strandi967 – 969Combined sources3
Helixi971 – 984Combined sources14
Helixi986 – 999Combined sources14
Beta strandi1001 – 1016Combined sources16
Helixi1022 – 1024Combined sources3
Beta strandi1026 – 1032Combined sources7
Beta strandi1038 – 1043Combined sources6
Beta strandi1047 – 1049Combined sources3
Helixi1051 – 1062Combined sources12
Helixi1067 – 1069Combined sources3
Turni1077 – 1079Combined sources3
Helixi1091 – 1115Combined sources25
Helixi1122 – 1131Combined sources10
Beta strandi1137 – 1142Combined sources6
Beta strandi1148 – 1150Combined sources3
Turni1151 – 1154Combined sources4
Beta strandi1155 – 1157Combined sources3
Beta strandi1160 – 1174Combined sources15
Turni1175 – 1177Combined sources3
Beta strandi1180 – 1190Combined sources11
Helixi1197 – 1215Combined sources19
Helixi1232 – 1234Combined sources3
Helixi1241 – 1243Combined sources3
Beta strandi1246 – 1252Combined sources7
Helixi1262 – 1264Combined sources3
Helixi1271 – 1276Combined sources6
Helixi1277 – 1293Combined sources17
Helixi1308 – 1314Combined sources7
Helixi1318 – 1322Combined sources5
Helixi1328 – 1330Combined sources3

3D structure databases

ProteinModelPortaliQ06278
SMRiQ06278
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 922Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST88
Domaini236 – 421FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST186

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni806 – 807Molybdopterin bindingCombined sources2 Publications2
Regioni1088 – 1091Molybdopterin bindingCombined sources2 Publications4

Sequence similaritiesi

Belongs to the xanthine dehydrogenase family.Curated

Phylogenomic databases

eggNOGiKOG0430 Eukaryota
COG4630 LUCA
COG4631 LUCA
GeneTreeiENSGT00390000003772
HOGENOMiHOG000191197
HOVERGENiHBG004182
InParanoidiQ06278
KOiK00157
OMAiTQSMLVV
OrthoDBiEOG091G01AW
PhylomeDBiQ06278
TreeFamiTF353036

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
IPR014313 Aldehyde_oxidase
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_2
IPR036318 FAD-bd_2-like_sf
IPR002346 Mopterin_DH_FAD-bd
IPR022407 OxRdtase_Mopterin_BS
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
TIGRFAMsiTIGR02969 mam_aldehyde_ox, 1 hit
PROSITEiView protein in PROSITE
PS00197 2FE2S_FER_1, 1 hit
PS51085 2FE2S_FER_2, 1 hit
PS51387 FAD_PCMH, 1 hit
PS00559 MOLYBDOPTERIN_EUK, 1 hit

Sequencei

Sequence statusi: Complete.

Q06278-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRASELLFY VNGRKVIEKN VDPETMLLPY LRKKLRLTGT KYGCGGGGCG 
        60         70         80         90        100
ACTVMISRYN PITKRIRHHP ANACLIPICS LYGAAVTTVE GIGSTHTRIH 
       110        120        130        140        150
PVQERIAKCH GTQCGFCTPG MVMSIYTLLR NHPEPTLDQL TDALGGNLCR 
       160        170        180        190        200
CTGYRPIIDA CKTFCKTSGC CQSKENGVCC LDQGINGLPE FEEGSKTSPK 
       210        220        230        240        250
LFAEEEFLPL DPTQELIFPP ELMIMAEKQS QRTRVFGSER MMWFSPVTLK 
       260        270        280        290        300
ELLEFKFKYP QAPVIMGNTS VGPEVKFKGV FHPVIISPDR IEELSVVNHA 
       310        320        330        340        350
YNGLTLGAGL SLAQVKDILA DVVQKLPEEK TQMYHALLKH LGTLAGSQIR 
       360        370        380        390        400
NMASLGGHII SRHPDSDLNP ILAVGNCTLN LLSKEGKRQI PLNEQFLSKC 
       410        420        430        440        450
PNADLKPQEI LVSVNIPYSR KWEFVSAFRQ AQRQENALAI VNSGMRVFFG 
       460        470        480        490        500
EGDGIIRELC ISYGGVGPAT ICAKNSCQKL IGRHWNEQML DIACRLILNE 
       510        520        530        540        550
VSLLGSAPGG KVEFKRTLII SFLFKFYLEV SQILKKMDPV HYPSLADKYE 
       560        570        580        590        600
SALEDLHSKH HCSTLKYQNI GPKQHPEDPI GHPIMHLSGV KHATGEAIYC 
       610        620        630        640        650
DDMPLVDQEL FLTFVTSSRA HAKIVSIDLS EALSMPGVVD IMTAEHLSDV 
       660        670        680        690        700
NSFCFFTEAE KFLATDKVFC VGQLVCAVLA DSEVQAKRAA KRVKIVYQDL 
       710        720        730        740        750
EPLILTIEES IQHNSSFKPE RKLEYGNVDE AFKVVDQILE GEIHMGGQEH 
       760        770        780        790        800
FYMETQSMLV VPKGEDQEMD VYVSTQFPKY IQDIVASTLK LPANKVMCHV 
       810        820        830        840        850
RRVGGAFGGK VLKTGIIAAV TAFAANKHGR AVRCVLERGE DMLITGGRHP 
       860        870        880        890        900
YLGKYKAGFM NDGRILALDM EHYSNAGASL DESLFVIEMG LLKMDNAYKF 
       910        920        930        940        950
PNLRCRGWAC RTNLPSNTAF RGFGFPQAAL ITESCITEVA AKCGLSPEKV 
       960        970        980        990       1000
RIINMYKEID QTPYKQEINA KNLIQCWREC MAMSSYSLRK VAVEKFNAEN 
      1010       1020       1030       1040       1050
YWKKKGLAMV PLKFPVGLGS RAAGQAAALV HIYLDGSVLV THGGIEMGQG 
      1060       1070       1080       1090       1100
VHTKMIQVVS RELRMPMSNV HLRGTSTETV PNANISGGSV VADLNGLAVK 
      1110       1120       1130       1140       1150
DACQTLLKRL EPIISKNPKG TWKDWAQTAF DESINLSAVG YFRGYESDMN 
      1160       1170       1180       1190       1200
WEKGEGQPFE YFVYGAACSE VEIDCLTGDH KNIRTDIVMD VGCSINPAID 
      1210       1220       1230       1240       1250
IGQIEGAFIQ GMGLYTIEEL NYSPQGILHT RGPDQYKIPA ICDMPTELHI 
      1260       1270       1280       1290       1300
ALLPPSQNSN TLYSSKGLGE SGVFLGCSVF FAIHDAVSAA RQERGLHGPL 
      1310       1320       1330 
TLNSPLTPEK IRMACEDKFT KMIPRDEPGS YVPWNVPI
Length:1,338
Mass (Da):147,918
Last modified:November 25, 2008 - v2
Checksum:i2AB5E543F18C9261
GO

Sequence cautioni

The sequence AAA96650 differs from that shown. Reason: Frameshift at positions 284, 286, 294 and 302.Curated
The sequence AAB83966 differs from that shown. Reason: Frameshift at positions 284, 286, 294 and 302.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti41K → P in AAA96650 (PubMed:8248161).Curated1
Sequence conflicti41K → P in AAB83966 (Ref. 2) Curated1
Sequence conflicti127T → P in AAA96650 (PubMed:8248161).Curated1
Sequence conflicti127T → P in AAB83966 (Ref. 2) Curated1
Sequence conflicti152T → H in AAA96650 (PubMed:8248161).Curated1
Sequence conflicti152T → H in AAB83966 (Ref. 2) Curated1
Sequence conflicti227E → D in AAA96650 (PubMed:8248161).Curated1
Sequence conflicti227E → D in AAB83966 (Ref. 2) Curated1
Sequence conflicti251E → D in AAA96650 (PubMed:8248161).Curated1
Sequence conflicti418Y → I in AAA96650 (PubMed:8248161).Curated1
Sequence conflicti418Y → I in AAB83966 (Ref. 2) Curated1
Sequence conflicti501V → L in AAB83966 (Ref. 2) Curated1
Sequence conflicti627I → N in AAB83966 (Ref. 2) Curated1
Sequence conflicti929A → V in AAA96650 (PubMed:8248161).Curated1
Sequence conflicti929A → V in AAB83966 (Ref. 2) Curated1
Sequence conflicti1019G → A in AAA96650 (PubMed:8248161).Curated1
Sequence conflicti1019G → A in AAB83966 (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_061136314Q → R. Corresponds to variant dbSNP:rs58185012Ensembl.1
Natural variantiVAR_047517802R → C Decreases homodimerization but nearly no effect on kinetic parameters. 1 PublicationCorresponds to variant dbSNP:rs41309768Ensembl.1
Natural variantiVAR_070256921R → H Increases homodimerization; abolishes enzymatic activity on phenanthridine; decreases turnover number with benzaldehyde, phtalazine and chloroquinazolinone as substrate, while nearly no effect on the KM. 1 PublicationCorresponds to variant dbSNP:rs56199635Ensembl.1
Natural variantiVAR_0702571135N → S Increases homodimerization and turnover number with phenanthridine as substrate; nearly no effect on kinetic parameters with benzaldehyde, phtalazine and chloroquinazolinone as substrate. 1 PublicationCorresponds to variant dbSNP:rs55754655Ensembl.1
Natural variantiVAR_0702581271S → L No effect on dimerization; no effect on oxidase activity. 2 PublicationsCorresponds to variant dbSNP:rs141786030Ensembl.1
Natural variantiVAR_0475181297H → R Increases homodimerization and turnover number with phenanthridine as substrate; nearly no effect on kinetic parameters with benzaldehyde, phtalazine and chloroquinazolinone as substrate. 1 PublicationCorresponds to variant dbSNP:rs3731722Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11005 mRNA Translation: AAA96650.1 Frameshift.
AF017060
, AF009441, AF009442, AF009443, AF009444, AF009445, AF009446, AF009447, AF009448, AF009449, AF009450, AF009451, AF009452, AF009453, AF009454, AF009455, AF009456, AF009457, AF009458, AF009459, AF009460, AF009461, AF009462, AF009463, AF009464, AF009465, AF009466, AF009467, AF009468, AF009469, AF009470, AF009471, AF009472, AF009473, AF009474 Genomic DNA Translation: AAB83966.1 Frameshift.
AF010260 Genomic DNA Translation: AAB83968.1
AB046692 mRNA Translation: BAB40305.1
AC007163 Genomic DNA Translation: AAX93285.1
AC080164 Genomic DNA Translation: AAY24265.1
CH471063 Genomic DNA Translation: EAW70209.1
BC117179 mRNA Translation: AAI17180.1
BC117181 mRNA Translation: AAI17182.1
CCDSiCCDS33360.1
PIRiA49634
RefSeqiNP_001150.3, NM_001159.3
UniGeneiHs.406238

Genome annotation databases

EnsembliENST00000374700; ENSP00000363832; ENSG00000138356
GeneIDi316
KEGGihsa:316
UCSCiuc002uvx.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiAOXA_HUMAN
AccessioniPrimary (citable) accession number: Q06278
Secondary accession number(s): O14765
, Q53RR8, Q53TV3, Q9BYF0, Q9UPG6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 25, 2008
Last modified: July 18, 2018
This is version 180 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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