AOX1

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.2 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:23263164).1 Publication

Catalytic activityⁱ

An aldehyde + H₂O + O₂ = a carboxylate + H₂O₂.1 Publication

Retinal + O₂ + H₂O = retinoate + H₂O₂.1 Publication

Cofactorⁱ

Protein has several cofactor binding sites:

[2Fe-2S] cluster
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:O54754 (AOXA_MOUSE)
Note: Binds 2 [2Fe-2S] clusters per subunit.
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:O54754 (AOXA_MOUSE)
FAD
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:O54754 (AOXA_MOUSE)
Note: Binds 1 FAD per subunit.
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:O54754 (AOXA_MOUSE)
Mo-molybdopterin
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:O54754 (AOXA_MOUSE)
Note: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:O54754 (AOXA_MOUSE)

Enzyme regulationⁱ

Inhibited by menadione and isovanillin. Not inhibited by allopurinol, a xanthine dehydrogenase potent inhibitor.1 Publication

Kineticsⁱ

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	43	Iron-sulfur 1 (2Fe-2S)By similarity	1
Metal bindingⁱ	48	Iron-sulfur 1 (2Fe-2S)By similarity	1
Metal bindingⁱ	51	Iron-sulfur 1 (2Fe-2S)By similarity	1
Metal bindingⁱ	73	Iron-sulfur 1 (2Fe-2S)By similarity	1
Binding siteⁱ	112	MolybdopterinBy similarity	1
Metal bindingⁱ	113	Iron-sulfur 2 (2Fe-2S)By similarity	1
Metal bindingⁱ	116	Iron-sulfur 2 (2Fe-2S)By similarity	1
Metal bindingⁱ	148	Iron-sulfur 2 (2Fe-2S)By similarity	1
Metal bindingⁱ	150	Iron-sulfur 2 (2Fe-2S)By similarity	1
Binding siteⁱ	150	MolybdopterinBy similarity	1
Binding siteⁱ	343	FAD; via amide nitrogenBy similarity	1
Binding siteⁱ	352	FADBy similarity	1
Binding siteⁱ	356	FADBy similarity	1
Binding siteⁱ	365	FADBy similarity	1
Binding siteⁱ	409	FAD; via amide nitrogen and carbonyl oxygenBy similarity	1
Binding siteⁱ	1041	Molybdopterin; via carbonyl oxygenBy similarity	1
Binding siteⁱ	1197	MolybdopterinBy similarity	1
Binding siteⁱ	1262	Molybdopterin; via carbonyl oxygenBy similarity	1
Active siteⁱ	1264	Proton acceptor; for azaheterocycle hydroxylase activityBy similarity	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	262 – 269	FADBy similarity		8

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
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
protein homodimerization activity Source: UniProtKB
retinal oxidase activity Source: UniProtKB

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

drug metabolic process Source: UniProtKB
oxidation-reduction process Source: UniProtKB

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Ligand	2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum

Enzyme and pathway databases

SABIO-RKⁱ	H9TB17.

SABIO-RKⁱ

H9TB17.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Aldehyde oxidase 1By similarity (EC:1.2.3.11 Publication) Alternative name(s): Azaheterocycle hydroxylase 1 (EC:1.17.3.-)
Gene namesⁱ	Name:AOX1By similarity Synonyms:AO
Organismⁱ	Cavia porcellus (Guinea pig)
Taxonomic identifierⁱ	10141 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Hystricomorpha › Caviidae › Cavia
Proteomesⁱ	UP000005447 Componentⁱ: Unassembled WGS sequence

Keywords - Cellular componentⁱ

Cytoplasm

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000425242	1 – 1332	Aldehyde oxidase 1Add BLAST		1332

Expressionⁱ

Tissue specificityⁱ

Expressed in liver.1 Publication

Interactionⁱ

Subunit structureⁱ

Homodimer.By similarity

GO - Molecular functionⁱ

protein homodimerization activity Source: UniProtKB

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

STRINGⁱ	10141.ENSCPOP00000021102.

STRINGⁱ

10141.ENSCPOP00000021102.

Structureⁱ

3D structure databases

SMRⁱ	H9TB17.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	4 – 91	2Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST		88
Domainⁱ	234 – 419	FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST		186

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	800 – 801	Molybdopterin bindingBy similarity		2
Regionⁱ	1082 – 1085	Molybdopterin bindingBy similarity		4

Sequence similaritiesⁱ

Belongs to the xanthine dehydrogenase family.Curated

Phylogenomic databases

eggNOGⁱ	KOG0430. Eukaryota. COG4631. LUCA.

eggNOGⁱ

KOG0430. Eukaryota.
COG4631. LUCA.

Family and domain databases

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. 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.
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.
PIRSFⁱ	PIRSF000127. Xanthine_DH. 1 hit.
SMARTⁱ	View protein in SMART SM01008. Ald_Xan_dh_C. 1 hit. SM01092. CO_deh_flav_C. 1 hit.
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.
TIGRFAMsⁱ	TIGR02969. mam_aldehyde_ox. 1 hit.
PROSITEⁱ	View 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.

H9TB17-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MEPSTLYFYV NGRRVTEKNV DPETMLLPYL GRNLRLTGTK YGCGGGGCGA 
        60         70         80         90        100
CTVMVSRYDR GTGQIRHYPA CACLTPLCSL HGAAVTTVEG VGSTRTRLHP 
       110        120        130        140        150
VQERIAKSHG TQCGFCTPGM VMSLYALLRS HPQPSEEQLL EALAGNLCRC 
       160        170        180        190        200
TGYRPILDAG KTFCKTSGCC QSKENGVCCL DQGVNGVQEA EGEQTSQELC 
       210        220        230        240        250
SEEEFVPLDP TQELIFPPEL MILAQKQPQK SRVFTGDRVT WISPVTLKDL 
       260        270        280        290        300
LEAKAKNPRA PVVMGNTSVG PEMKFKGVFH PVIISPDGIE ELSVIKQGNE 
       310        320        330        340        350
GLTLGAGLSL AQVQDVLADV VQQLPEEKTQ TLCALLKQLR TLAGSQIRNM 
       360        370        380        390        400
ASLGGHIMSR HLDSDLNPVL AAASCTLHVP SQEGDRQIPL DEHFLSRSPS 
       410        420        430        440        450
ADLRPQEVLL SVTIPYSRKW EFVSAFRQAQ RKRSARAIVN VGMRVFFGAG 
       460        470        480        490        500
DGVISELCIL YGGVGPAIVC ATDACRKLVG RHWTEEMLDE ACRLVLGEVA 
       510        520        530        540        550
IPGAAPGGRV EFRRTLLVSF LFRFYLQVSQ SLSRMDPGRY PSLVGKYESA 
       560        570        580        590        600
LEDLCLGHHQ RTFELQSADA KQLPQDPIGR PIMHLSGIKH TTGEAIYCDD 
       610        620        630        640        650
MPLVDRELSL AFVTSSRAHA AILSMDLSEA LSLPGVVDIV TAEHLGDANS 
       660        670        680        690        700
FAKETLLATD KVLCVGHLVC AVIADSEVQA KRAAEKVKIV YQDLEPLILT 
       710        720        730        740        750
IEEAIQHDSF FETERKLESG DVAEAFRTAE QVLEGSIHMG GQEHFYMETQ 
       760        770        780        790        800
SMLAVPKGED QEIDLYVSTQ FPTYIQEIVA STLKLPVNKV MCHVRRVGGA 
       810        820        830        840        850
FGGKVGKTAI LAAITAFAAL KHCRAVRCIL ERGEDMLITG GRHPYLGKYK 
       860        870        880        890        900
VGFRNNGQVV ALDMEHYSNA GSTLDESLMV VEMGLLKMEN AYKFPNLRCR 
       910        920        930        940        950
GHACKTNLPS NTALRGFGFP QSGLITEACI VEVAARCGLS PEEVREVNMY 
       960        970        980        990       1000
RGTEQTHYGQ EIHTQRLAQC WSECKAKATF SLRRAAVDRF NAGSPWKKRG 
      1010       1020       1030       1040       1050
LAMVPLKFPV GLGSVAMGQA AALVHVYLDG SVLLTHGGIE MGQGVHTKMI 
      1060       1070       1080       1090       1100
QVVSRELKMP MANVHLRGTS TETVPNANVS GGSVVADLNG LAVKDACQTL 
      1110       1120       1130       1140       1150
LKRLEPIISK NPKGTWKEWA QAAFDQSISL SAIGYFRGYD ADMDWEKGKG 
      1160       1170       1180       1190       1200
HPFEYFVYGA ACSEVEIDCL TGNHKNIRTD IVMDVGRSIN PALDLGQVEG 
      1210       1220       1230       1240       1250
AFIQGMGLYT SEELKYGPQG ALYTRGPDQY KIPAVCDVPA ELHVFFLPPS 
      1260       1270       1280       1290       1300
KNSNTLYSSK GLGESGVFLG CSVLFAIWDA VSAARRERGL PGTLALSCPL 
      1310       1320       1330 
TPEKIRMACE DRFTKMIPRD TPGSYVPWDV VV

Length:1,332

Mass (Da):145,275

Last modified:February 19, 2014 - v2

Checksum:ⁱ348556EBE581FE04

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	519	S → N in AFG18181 (PubMed:23263164).Curated	1
Sequence conflictⁱ	677	E → G in AFG18181 (PubMed:23263164).Curated	1
Sequence conflictⁱ	695	E → G in AFG18181 (PubMed:23263164).Curated	1
Sequence conflictⁱ	1137	R → T in AFG18181 (PubMed:23263164).Curated	1
Sequence conflictⁱ	1201	A → P in AFG18181 (PubMed:23263164).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	JQ280309 mRNA. Translation: AFG18181.1. AAKN02051283 Genomic DNA. No translation available.
NCBI Reference Sequences More...RefSeqⁱ	NP_001295371.1. NM_001308442.1.

Genome annotation databases

GeneIDⁱ	100720210.

GeneIDⁱ

100720210.

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
H9TB17	UPI0002573900 UPI000661BC89 A0A096P6K6	Cavia porcellus (Guinea pig)	1,332	UniRef90_H9TB17	Cluster: Aldehyde oxidase 1	4

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
H9TB17	O54754 UPI000A31516F Q9Z0U5 F1LRQ1 Q8R387 UPI00001706B6 G3X8P9 UPI000A30E028 UPI0005400924 UPI00038C56A9 +171	Mus musculus (Mouse) Mus caroli (Ryukyu mouse) (Ricefield mouse) Rattus norvegicus (Rat) Mus pahari (Gairdner's shrew-mouse) (Coelomys pahari) Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis) Microtus ochrogaster (Prairie vole) Monodelphis domestica (Gray short-tailed opossum) Phascolarctos cinereus (Koala) Gallus gallus (Chicken) Meleagris gallopavo (Wild turkey) And more	1,333	UniRef50_O54754	Cluster: Aldehyde oxidase 1	182

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	JQ280309 mRNA. Translation: AFG18181.1. AAKN02051283 Genomic DNA. No translation available.
NCBI Reference Sequences More...RefSeqⁱ	NP_001295371.1. NM_001308442.1.

3D structure databases

SMRⁱ	H9TB17.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	10141.ENSCPOP00000021102.

STRINGⁱ

10141.ENSCPOP00000021102.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

GeneIDⁱ	100720210.

GeneIDⁱ

100720210.

Organism-specific databases

CTDⁱ	316.

CTDⁱ

316.

Phylogenomic databases

eggNOGⁱ	KOG0430. Eukaryota. COG4631. LUCA.

eggNOGⁱ

KOG0430. Eukaryota.
COG4631. LUCA.

Enzyme and pathway databases

SABIO-RKⁱ	H9TB17.

SABIO-RKⁱ

H9TB17.

Family and domain databases

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. 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.
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.
PIRSFⁱ	PIRSF000127. Xanthine_DH. 1 hit.
SMARTⁱ	View protein in SMART SM01008. Ald_Xan_dh_C. 1 hit. SM01092. CO_deh_flav_C. 1 hit.
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.
TIGRFAMsⁱ	TIGR02969. mam_aldehyde_ox. 1 hit.
PROSITEⁱ	View 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.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	AOXA_CAVPO
Accessionⁱ	H9TB17Primary (citable) accession number: H9TB17 Secondary accession number(s): H0WDM9
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	February 19, 2014
	Last sequence update:	February 19, 2014
	Last modified:	March 28, 2018
	This is version 34 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

UniProtKB

UniParc

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Proteomes

Annotation systems

Supporting data

UniProtKB - H9TB17 (AOXA_CAVPO)

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Aldehyde oxidase 1

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<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

Miscellaneous

<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi

<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

Sites

Regions

<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

<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 - Biological processi

Enzyme and pathway databases

<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 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

Other locations

Cytosol

<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

<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 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>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

Protein-protein interaction databases

<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

<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

Region

<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

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<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

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

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Functionⁱ

Enzyme regulationⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ