AOXD_MOUSE
ID AOXD_MOUSE Reviewed; 1336 AA.
AC Q3TYQ9; Q8VI17;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Aldehyde oxidase 4;
DE EC=1.2.3.1 {ECO:0000269|PubMed:18981221};
DE AltName: Full=Aldehyde oxidase homolog 2;
DE AltName: Full=Azaheterocycle hydroxylase 4;
DE EC=1.17.3.-;
DE AltName: Full=Retinal oxidase {ECO:0000305|PubMed:18981221};
GN Name=Aox4; Synonyms=Aoh2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=11562361; DOI=10.1074/jbc.m105744200;
RA Terao M., Kurosaki M., Marini M., Vanoni M.A., Saltini G., Bonetto V.,
RA Bastone A., Federico C., Saccone S., Fanelli R., Salmona M., Garattini E.;
RT "Purification of the aldehyde oxidase homolog 1 (AOH1) protein and cloning
RT of the AOH1 and aldehyde oxidase homolog 2 (AOH2) genes. Identification of
RT a novel molybdo-flavoprotein gene cluster on mouse chromosome 1.";
RL J. Biol. Chem. 276:46347-46363(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION AS RETINAL OXIDASE, CATALYTIC ACTIVITY, KINETIC PARAMETERS,
RP SUBSTRATE SPECIFICITY, TISSUE SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18981221; DOI=10.1128/mcb.01385-08;
RA Terao M., Kurosaki M., Barzago M.M., Fratelli M., Bagnati R., Bastone A.,
RA Giudice C., Scanziani E., Mancuso A., Tiveron C., Garattini E.;
RT "Role of the molybdoflavoenzyme aldehyde oxidase homolog 2 in the
RT biosynthesis of retinoic acid: generation and characterization of a
RT knockout mouse.";
RL Mol. Cell. Biol. 29:357-377(2009).
RN [6]
RP TISSUE SPECIFICITY, AND IDENTIFICATION OF PARALOGS.
RX PubMed=23263164; DOI=10.1007/s00018-012-1229-5;
RA Kurosaki M., Bolis M., Fratelli M., Barzago M.M., Pattini L., Perretta G.,
RA Terao M., Garattini E.;
RT "Structure and evolution of vertebrate aldehyde oxidases: from gene
RT duplication to gene suppression.";
RL Cell. Mol. Life Sci. 70:1807-1830(2013).
CC -!- FUNCTION: Aldehyde oxidase able to catalyze the oxidation of
CC retinaldehyde into retinoate. Is responsible for the major all-trans-
CC retinaldehyde-metabolizing activity in the Harderian gland, and
CC contributes a significant amount of the same activity in the skin. Is
CC devoid of pyridoxal-oxidizing activity, in contrast to the other
CC aldehyde oxidases. Acts as a negative modulator of the epidermal
CC trophism. May be able to oxidize a wide variety of aldehydes into their
CC corresponding carboxylates and to hydroxylate azaheterocycles.
CC {ECO:0000269|PubMed:18981221}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2;
CC Xref=Rhea:RHEA:16829, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478,
CC ChEBI:CHEBI:29067; EC=1.2.3.1;
CC Evidence={ECO:0000269|PubMed:18981221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + retinal = H(+) + H2O2 + retinoate;
CC Xref=Rhea:RHEA:56736, ChEBI:CHEBI:15035, ChEBI:CHEBI:15036,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240; Evidence={ECO:0000269|PubMed:18981221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinal + H2O + O2 = all-trans-retinoate + H(+) +
CC H2O2; Xref=Rhea:RHEA:22520, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17898,
CC ChEBI:CHEBI:35291; EC=1.2.3.1;
CC Evidence={ECO:0000269|PubMed:18981221};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:G3X982};
CC Note=Binds 2 [2Fe-2S] clusters per subunit.
CC {ECO:0000250|UniProtKB:G3X982};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:G3X982};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:G3X982};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000250|UniProtKB:G3X982};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000250|UniProtKB:G3X982};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.8 uM for all-trans-retinal (at 37 degrees Celsius and pH 7.4)
CC {ECO:0000269|PubMed:18981221};
CC Vmax=0.06 umol/min/mg enzyme with all-trans-retinal as substrate (at
CC 37 degrees Celsius and pH 7.4) {ECO:0000269|PubMed:18981221};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:G3X982}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18981221}.
CC -!- TISSUE SPECIFICITY: Highly expressed in Harderian glands and sebaceous
CC glands with detectable levels in the epidermis and other keratinized
CC epithelia (at protein level). Detected in testis. The expression is 3
CC times greater in females than in males. {ECO:0000269|PubMed:18981221,
CC ECO:0000269|PubMed:23263164}.
CC -!- INDUCTION: Repressed by testosterone in Harderian glands. In skin,
CC induced by UVB light. {ECO:0000269|PubMed:18981221}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable, fertile and born at the expected
CC Mendelian rate. However, they show a deficiency of retinoic acid
CC synthesis in both the Harderian gland and skin. The Harderian gland's
CC transcriptome of knockout mice demonstrates overall down-regulation of
CC direct retinoid-dependent genes as well as perturbations in pathways
CC controlling lipid homeostasis and cellular secretion, particularly in
CC sexually immature animals. The skin is characterized by thickening of
CC the epidermis in basal conditions and after UVB light exposure.
CC {ECO:0000269|PubMed:18981221}.
CC -!- MISCELLANEOUS: AOX genes evolved from a xanthine oxidoreductase
CC ancestral precursor via a series of gene duplication and
CC suppression/deletion events. Different animal species contain a
CC different complement of AOX genes encoding an equivalent number of AOX
CC isoenzymes. In mammals, the two extremes are represented by certain
CC rodents such as mice and rats, which are endowed with 4 AOX genes, and
CC by humans, whose genome is characterized by a single active gene
CC (PubMed:23263164). {ECO:0000305|PubMed:23263164}.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AF321814; AAL38126.1; -; Genomic_DNA.
DR EMBL; AF321780; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321781; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321782; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321783; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321784; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321785; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321786; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321787; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321788; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321789; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321790; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321791; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321792; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321793; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321794; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321795; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321796; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321797; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321798; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321799; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321800; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321801; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321802; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321803; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321804; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321805; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321806; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321807; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321808; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321809; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321810; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321811; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321812; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AF321813; AAL38126.1; JOINED; Genomic_DNA.
DR EMBL; AK158427; BAE34503.1; -; mRNA.
DR EMBL; AC025116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117975; AAI17976.1; -; mRNA.
DR CCDS; CCDS14970.1; -.
DR RefSeq; NP_076120.2; NM_023631.2.
DR AlphaFoldDB; Q3TYQ9; -.
DR SMR; Q3TYQ9; -.
DR STRING; 10090.ENSMUSP00000048929; -.
DR iPTMnet; Q3TYQ9; -.
DR PhosphoSitePlus; Q3TYQ9; -.
DR jPOST; Q3TYQ9; -.
DR MaxQB; Q3TYQ9; -.
DR PaxDb; Q3TYQ9; -.
DR PRIDE; Q3TYQ9; -.
DR ProteomicsDB; 281781; -.
DR DNASU; 71872; -.
DR Ensembl; ENSMUST00000040442; ENSMUSP00000048929; ENSMUSG00000038242.
DR GeneID; 71872; -.
DR KEGG; mmu:71872; -.
DR UCSC; uc007bbo.1; mouse.
DR CTD; 71872; -.
DR MGI; MGI:1919122; Aox4.
DR VEuPathDB; HostDB:ENSMUSG00000038242; -.
DR eggNOG; KOG0430; Eukaryota.
DR GeneTree; ENSGT00950000183114; -.
DR HOGENOM; CLU_001681_1_2_1; -.
DR InParanoid; Q3TYQ9; -.
DR OMA; AQSEVIC; -.
DR OrthoDB; 48717at2759; -.
DR PhylomeDB; Q3TYQ9; -.
DR TreeFam; TF353036; -.
DR BioGRID-ORCS; 71872; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Aox4; mouse.
DR PRO; PR:Q3TYQ9; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3TYQ9; protein.
DR Bgee; ENSMUSG00000038242; Expressed in tail skin and 59 other tissues.
DR Genevisible; Q3TYQ9; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0004031; F:aldehyde oxidase activity; ISS:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; ISA:MGI.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0030151; F:molybdenum ion binding; ISA:MGI.
DR GO; GO:0043546; F:molybdopterin cofactor binding; ISS:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH.
DR InterPro; IPR014313; Aldehyde_oxidase.
DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR005107; CO_DH_flav_C.
DR InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR PANTHER; PTHR11908; PTHR11908; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR Pfam; PF03450; CO_deh_flav_C; 1.
DR Pfam; PF00941; FAD_binding_5; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR PIRSF; PIRSF000127; Xanthine_DH; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SMART; SM01092; CO_deh_flav_C; 1.
DR SUPFAM; SSF47741; SSF47741; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF54665; SSF54665; 1.
DR SUPFAM; SSF55447; SSF55447; 1.
DR SUPFAM; SSF56003; SSF56003; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR TIGRFAMs; TIGR02969; mam_aldehyde_ox; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Cytoplasm; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding;
KW Molybdenum; Oxidoreductase; Reference proteome.
FT CHAIN 1..1336
FT /note="Aldehyde oxidase 4"
FT /id="PRO_0000425250"
FT DOMAIN 8..95
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 237..423
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT ACT_SITE 1267
FT /note="Proton acceptor; for azaheterocycle hydroxylase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:O54754"
FT BINDING 47
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 52
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 55
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 77
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 116
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 117
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 120
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 152
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 154
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 154
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 265..272
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 346
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 355
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 359
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 368
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 413
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 804..805
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 1045
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250"
FT BINDING 1086..1089
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 1201
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT BINDING 1265
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:Q06278"
FT CONFLICT 386
FT /note="Missing (in Ref. 1; AAL38126)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1336 AA; 148279 MW; F12D7DA84A31A717 CRC64;
MPSVSESDEL IFFVNGKKVI EKNPDPEKNL LFYTRKVLNL TGTKYSCGTG GCGACTVMVS
RYNPKTRKIH HYPATACLVP ICWLHGAAIT TVEGVGSIKK RVHPVQERLA KCHGTQCGFC
SPGMVMSIYT LLRNHPEPTP DQITEALGGN LCRCTGYRPI VESGKTFSQK STVCQMKGSG
KCCMDPDEKC LESREKKMCT KLYNEDEFQP FDPSQEPIFP PELIRMAEDP NKRRLTFQGK
RTTWIIPVTL NDLLELKASY PEAPLVMGNT TVGPGIKFND EFYPVFISPL GVPELNLMDT
TNNGVTIGAG YSLAQLKDTL DFLVSEQPKE KTKTFHALQK HLRTLAGPQI RNMATLGGHT
ASRPNFSDLN PILAAGNATI NVVSREGKDR QLPLNGPFLE KLPEADLKPE EVILSIFIPY
TAQWQFVSGL RLAQRQENAF AIVNAGMSVE FEEGTNTIKD LKMFFGSVAP TVVSASQTCK
QLIGRQWDDQ MLSDACQLVL QEIRIPPDAE GGMVEYRRTL IISLLFKFYL KVQRWLNEMD
PQKFPDIPGK FVSALDDFPI ETPQGIQMFQ CVDPKQPQKD PVGHPIMHQS GIKHATGEAI
FIDDMPPIDQ ELCLAVVTST RAHAKITSLD VSEALACPGV VDVITAEDVP GENDHNGEIL
YAQSEVICVG QIICTVAADT YIHAKEAAKR VKIAYDDIEP TIITIEEALE HNSFLSPEKK
IEQGNVDYAF KHVDQIVEGE IHVEGQEHFY METQTILAIP QTEDKEMVLH LGTQFPTHVQ
EFVSAALNVP RSRIACHMKR AGGAFGGKVT KPALLGAVCA VAANKTGRPI RFILERSDDM
LITAGRHPLL GKYKIGFMNN GEIRAADVEY YTNGGCTPDE SELVIEFVVL KSENTYHIPN
FRCRGRACKT NLPSNTAFRG FGFPQATVVV EAYIAAVASK CNLLPEEVRE INMYKKTSKT
AYKQTFNPEP LRRCWKECLE KSSFFARKKA AEEFNGNNYW KKRGLAVVPM KFSVAVPIAF
YNQAAALVHI FLDGSVLLTH GGCELGQGLH TKMIQVASRE LNVPKSYVHF SETSTTTVPN
SAFTAGSMGA DINGKAVQNA CQILMDRLRP IIRKNPKGKW EEWIKMAFEE SISLSATGYF
KGYQTNMDWK KEEGDPYPYY VYGAACSEVE VDCLTGAHKL LRTDIFVDAA FSINPALDIG
QVEGAFIQGM GFYTTEELKY SPKGVLYSRG PEDYKIPTIT EIPEEFYVTL VHSRNPIAIY
SSKGLGEAGM FLGSSVLFAI YDAVTTARKE RGLSDIFPLN SPATPEVIRM ACTDQFTEMI
PRDDPSTFTP WSIHVS
