ID   XDH1_ARATH              Reviewed;        1361 AA.
AC   Q8GUQ8; Q9SW46;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 144.
DE   RecName: Full=Xanthine dehydrogenase 1;
DE            Short=AtXDH1;
DE            EC=1.17.1.4 {ECO:0000269|PubMed:14726515};
GN   Name=XDH1; OrderedLocusNames=At4g34890; ORFNames=T11I11.130;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RX   PubMed=14726515; DOI=10.1074/jbc.m312929200;
RA   Hesberg C., Haensch R., Mendel R.R., Bittner F.;
RT   "Tandem orientation of duplicated xanthine dehydrogenase genes from
RT   Arabidopsis thaliana: differential gene expression and enzyme activities.";
RL   J. Biol. Chem. 279:13547-13554(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=15941399; DOI=10.1111/j.1365-313x.2005.02422.x;
RA   Yesbergenova Z., Yang G., Oron E., Soffer D., Fluhr R., Sagi M.;
RT   "The plant Mo-hydroxylases aldehyde oxidase and xanthine dehydrogenase have
RT   distinct reactive oxygen species signatures and are induced by drought and
RT   abscisic acid.";
RL   Plant J. 42:862-876(2005).
RN   [5]
RP   FUNCTION.
RX   PubMed=17872919; DOI=10.1093/pcp/pcm119;
RA   Nakagawa A., Sakamoto S., Takahashi M., Morikawa H., Sakamoto A.;
RT   "The RNAi-mediated silencing of xanthine dehydrogenase impairs growth and
RT   fertility and accelerates leaf senescence in transgenic Arabidopsis
RT   plants.";
RL   Plant Cell Physiol. 48:1484-1495(2007).
RN   [6]
RP   FUNCTION.
RX   PubMed=18266920; DOI=10.1111/j.1365-313x.2008.03440.x;
RA   Brychkova G., Alikulov Z., Fluhr R., Sagi M.;
RT   "A critical role for ureides in dark and senescence-induced purine
RT   remobilization is unmasked in the Atxdh1 Arabidopsis mutant.";
RL   Plant J. 54:496-509(2008).
RN   [7]
RP   FUNCTION.
RX   PubMed=20153325; DOI=10.1016/j.febslet.2010.02.023;
RA   Watanabe S., Nakagawa A., Izumi S., Shimada H., Sakamoto A.;
RT   "RNA interference-mediated suppression of xanthine dehydrogenase reveals
RT   the role of purine metabolism in drought tolerance in Arabidopsis.";
RL   FEBS Lett. 584:1181-1186(2010).
RN   [8]
RP   FUNCTION, AND MUTAGENESIS OF TRP-364; TYR-421; GLU-831; ARG-909 AND
RP   GLU-1297.
RX   PubMed=19915948; DOI=10.1007/s11103-009-9570-2;
RA   Zarepour M., Kaspari K., Stagge S., Rethmeier R., Mendel R.R., Bittner F.;
RT   "Xanthine dehydrogenase AtXDH1 from Arabidopsis thaliana is a potent
RT   producer of superoxide anions via its NADH oxidase activity.";
RL   Plant Mol. Biol. 72:301-310(2010).
CC   -!- FUNCTION: Key enzyme involved in purine catabolism. Catalyzes the
CC       oxidation of hypoxanthine to xanthine and the oxidation of xanthine to
CC       urate. Regulates the level of ureides and plays an important role
CC       during plant growth and development, senescence and response to
CC       stresses. Possesses NADH oxidase activity and may contribute to the
CC       generation of superoxide anions in planta.
CC       {ECO:0000269|PubMed:14726515, ECO:0000269|PubMed:15941399,
CC       ECO:0000269|PubMed:17872919, ECO:0000269|PubMed:18266920,
CC       ECO:0000269|PubMed:19915948, ECO:0000269|PubMed:20153325}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NAD(+) + xanthine = H(+) + NADH + urate;
CC         Xref=Rhea:RHEA:16669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17712, ChEBI:CHEBI:17775, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.17.1.4;
CC         Evidence={ECO:0000269|PubMed:14726515};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + hypoxanthine + NAD(+) = H(+) + NADH + xanthine;
CC         Xref=Rhea:RHEA:24670, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17368, ChEBI:CHEBI:17712, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.17.1.4;
CC         Evidence={ECO:0000269|PubMed:14726515};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC       Note=Binds 2 [2Fe-2S] clusters. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250};
CC       Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC       {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:14726515}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC       siliques. {ECO:0000269|PubMed:14726515}.
CC   -!- INDUCTION: By salt and drought stresses, and abscisic (ABA) treatment.
CC       Down-regulated by cold and freezing stresses.
CC       {ECO:0000269|PubMed:14726515, ECO:0000269|PubMed:15941399}.
CC   -!- MISCELLANEOUS: Plants silencing simultaneously XDH1 and XDH2 show
CC       reduced growth, impaired silique development, increased seed sterility,
CC       precocious senescence of mature leaves and overaccumulation of
CC       xanthine. {ECO:0000305|PubMed:17872919}.
CC   -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB45450.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB80206.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY171562; AAO11781.1; -; mRNA.
DR   EMBL; AL079347; CAB45450.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161586; CAB80206.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE86434.1; -; Genomic_DNA.
DR   PIR; T10235; T10235.
DR   RefSeq; NP_195215.2; NM_119655.4.
DR   AlphaFoldDB; Q8GUQ8; -.
DR   SMR; Q8GUQ8; -.
DR   BioGRID; 14923; 2.
DR   STRING; 3702.Q8GUQ8; -.
DR   iPTMnet; Q8GUQ8; -.
DR   PaxDb; 3702-AT4G34890-1; -.
DR   ProteomicsDB; 243096; -.
DR   EnsemblPlants; AT4G34890.1; AT4G34890.1; AT4G34890.
DR   GeneID; 829641; -.
DR   Gramene; AT4G34890.1; AT4G34890.1; AT4G34890.
DR   KEGG; ath:AT4G34890; -.
DR   Araport; AT4G34890; -.
DR   TAIR; AT4G34890; XDH1.
DR   eggNOG; KOG0430; Eukaryota.
DR   HOGENOM; CLU_001681_1_2_1; -.
DR   InParanoid; Q8GUQ8; -.
DR   OMA; PHPTQER; -.
DR   OrthoDB; 761229at2759; -.
DR   PhylomeDB; Q8GUQ8; -.
DR   BioCyc; ARA:AT4G34890-MONOMER; -.
DR   BioCyc; MetaCyc:AT4G34890-MONOMER; -.
DR   BRENDA; 1.17.1.4; 399.
DR   PRO; PR:Q8GUQ8; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8GUQ8; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004854; F:xanthine dehydrogenase activity; IDA:TAIR.
DR   GO; GO:0006145; P:purine nucleobase catabolic process; IMP:TAIR.
DR   GO; GO:0000302; P:response to reactive oxygen species; IMP:TAIR.
DR   GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR   GO; GO:0042554; P:superoxide anion generation; IMP:TAIR.
DR   GO; GO:0046110; P:xanthine metabolic process; IMP:TAIR.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR   Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4.
DR   Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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-like.
DR   InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR   InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
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; XANTHINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11908:SF100; XANTHINE DEHYDROGENASE; 1.
DR   Pfam; PF01315; Ald_Xan_dh_C; 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   Pfam; PF02738; MoCoBD_1; 1.
DR   Pfam; PF20256; MoCoBD_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; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR   SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR   SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   Genevisible; Q8GUQ8; AT.
PE   1: Evidence at protein level;
KW   2Fe-2S; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..1361
FT                   /note="Xanthine dehydrogenase 1"
FT                   /id="PRO_0000417457"
FT   DOMAIN          15..101
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   DOMAIN          257..442
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   ACT_SITE        1297
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         58
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         61
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         83
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         123
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         126
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         159
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         161
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         285..292
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         365
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         375..379
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         388
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         432
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         450
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         796
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000250"
FT   BINDING         827
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000250"
FT   BINDING         831
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         909
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         941
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000250"
FT   BINDING         943
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1039
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1108
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         364
FT                   /note="W->A: Decreases activity 8-fold."
FT                   /evidence="ECO:0000269|PubMed:19915948"
FT   MUTAGEN         421
FT                   /note="Y->A: Decreases activity 4-fold."
FT                   /evidence="ECO:0000269|PubMed:19915948"
FT   MUTAGEN         831
FT                   /note="E->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:19915948"
FT   MUTAGEN         909
FT                   /note="R->A: Decreases activity 12-fold."
FT                   /evidence="ECO:0000269|PubMed:19915948"
FT   MUTAGEN         1297
FT                   /note="E->A: Decreases activity 40-fold."
FT                   /evidence="ECO:0000269|PubMed:19915948"
SQ   SEQUENCE   1361 AA;  149196 MW;  BF72FE23A1D59C88 CRC64;
     MGSLKKDGEI GDEFTEALLY VNGVRRVLPD GLAHMTLLEY LRDLGLTGTK LGCGEGGCGA
     CTVMVSSYDR KSKTSVHYAV NACLAPLYSV EGMHVISIEG LGHRKLGLHP VQESLASSHG
     SQCGFCTPGF IMSMYSLLRS SKNSPSEEEI EECLAGNLCR CTGYRPIVDA FRVFAKSDDA
     LYCGVSSLSL QDGSTICPST GKPCSCGSKT TNEVASCNED RFQSISYSDI DGAKYTDKEL
     IFPPELLLRK LTPLKLRGNG GITWYRPVCL QNLLELKANY PDAKLLVGNT EVGIEMRLKR
     LQYQVLISVA QVPELNALNV NDNGIEVGSA LRLSELLRLF RKIVKERPAH ETSACKAFIE
     QLKWFAGTQI RNVACIGGNI CTASPISDLN PLWMASRAEF RITNCNGDVR SIPAKDFFLG
     YRKVDMGSNE ILLSVFLPWT RPLEYVKEFK QAHRRDDDIA IVNGGMRVFL EDKGQQLFVS
     DASIAYGGVA PLSLCARKTE EFLIGKNWNK DLLQDALKVI QSDVVIKEDA PGGMVEFRKS
     LTLSFFFKFF LWVSHNVNNA NSAIETFPPS HMSAVQPVPR LSRIGKQDYE TVKQGTSVGS
     SEVHLSARMQ VTGEAEYTDD TPVPPNTLHA AFVLSKVPHA RILSIDDSAA KSSSGFVGLF
     LAKDIPGDNM IGPIVPDEEL FATDVVTCVG QVIGVVVADT HENAKTAAGK VDVRYEELPA
     ILSIKEAINA KSFHPNTEKR LRKGDVELCF QSGQCDRVIE GEVQMGGQEH FYLEPNGSLV
     WTVDGGSEVH MISSTQAPQK HQKYVSHVLG LPMSKVVCKT KRIGGGFGGK ETRSAFIAAA
     ASVPSYLLNR PVKLILDRDV DMMITGHRHS FLGKYKVGFT NEGKILALDL EIYNNGGNSL
     DLSLSVLERA MFHSDNVYEI PHVRIVGNVC FTNFPSNTAF RGFGGPQGML ITENWIQRIA
     AELNKSPEEI KEMNFQVEGS VTHYCQTLQH CTLHQLWKEL KVSCNFLKAR READEFNSHN
     RWKKRGVAMV PTKFGISFTT KFMNQAGALV HVYTDGTVLV THGGVEMGQG LHTKVAQVAA
     SAFNIPLSSV FVSETSTDKV PNASPTAASA SSDMYGAAVL DACEQIIARM EPVASKHNFN
     TFTELVSACY FQRIDLSAHG FHIVPDLGFD WISGKGNAFR YYTYGAAFAE VEIDTLTGDF
     HTRAADIMLD LGYSLNPAID VGQIEGAFVQ GLGWVALEEL KWGDAAHKWI KPGSLLTCGP
     GNYKIPSIND MPFNLNVSLL KGNPNTKAIH SSKAVGEPPF FLASSVFFAI KEAIKAARTE
     VGLTDWFPLE SPATPERIRM ACFDEFSAPF VNSDFYPNLS V
//