DDAH1_HUMAN
ID DDAH1_HUMAN Reviewed; 285 AA.
AC O94760; Q5HYC8; Q86XK5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=N(G),N(G)-dimethylarginine dimethylaminohydrolase 1;
DE Short=DDAH-1;
DE Short=Dimethylarginine dimethylaminohydrolase 1;
DE EC=3.5.3.18;
DE AltName: Full=DDAHI;
DE AltName: Full=Dimethylargininase-1;
GN Name=DDAH1; Synonyms=DDAH;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 2-12 AND 35-50,
RP ABSENCE OF BOUND ZINC, AND ACETYLATION AT ALA-2.
RC TISSUE=Kidney, and Liver;
RX PubMed=9874257; DOI=10.1046/j.1432-1327.1998.2580863.x;
RA Kimoto M., Miyatake S., Sasagawa T., Yamashita H., Okita M., Oka T.,
RA Ogawa T., Tsuji H.;
RT "Purification, cDNA cloning and expression of human NG,NG-dimethylarginine
RT dimethylaminohydrolase.";
RL Eur. J. Biochem. 258:863-868(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=10493931; DOI=10.1042/bj3430209;
RA Leiper J.M., Santa Maria J., Chubb A., MacAllister R.J., Charles I.G.,
RA Whitley G.S., Vallance P.;
RT "Identification of two human dimethylarginine dimethylaminohydrolases with
RT distinct tissue distributions and homology with microbial arginine
RT deiminases.";
RL Biochem. J. 343:209-214(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Endometrial cancer;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, Kidney, Stomach, and Testis;
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 [7]
RP PROTEIN SEQUENCE OF 20-31; 46-57; 112-136; 150-196; 212-230 AND 268-281,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18171027; DOI=10.1021/bi701659n;
RA Forbes S.P., Druhan L.J., Guzman J.E., Parinandi N., Zhang L.,
RA Green-Church K.B., Cardounel A.J.;
RT "Mechanism of 4-HNE mediated inhibition of hDDAH-1: implications in NO
RT regulation.";
RL Biochemistry 47:1819-1826(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-284 IN COMPLEXES WITH CITRULLINE
RP AND INHIBITOR L-257.
RX PubMed=17273169; DOI=10.1038/nm1543;
RA Leiper J., Nandi M., Torondel B., Murray-Rust J., Malaki M., O'Hara B.,
RA Rossiter S., Anthony S., Madhani M., Selwood D., Smith C.,
RA Wojciak-Stothard B., Rudiger A., Stidwill R., McDonald N.Q., Vallance P.;
RT "Disruption of methylarginine metabolism impairs vascular homeostasis.";
RL Nat. Med. 13:198-203(2007).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH
RP N-1-IMINOPROPYL-L-ORNITHINE, CATALYTIC ACTIVITY, ZINC-BINDING, ACTIVITY
RP REGULATION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE,
RP MUTAGENESIS OF LEU-30; GLU-78 AND LEU-271, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19663506; DOI=10.1021/bi9007098;
RA Wang Y., Monzingo A.F., Hu S., Schaller T.H., Robertus J.D., Fast W.;
RT "Developing dual and specific inhibitors of dimethylarginine
RT dimethylaminohydrolase-1 and nitric oxide synthase: toward a targeted
RT polypharmacology to control nitric oxide.";
RL Biochemistry 48:8624-8635(2009).
CC -!- FUNCTION: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-
CC monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has
CC therefore a role in the regulation of nitric oxide generation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(omega),N(omega)-dimethyl-L-arginine = dimethylamine +
CC L-citrulline; Xref=Rhea:RHEA:17305, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57743, ChEBI:CHEBI:58040, ChEBI:CHEBI:58326; EC=3.5.3.18;
CC Evidence={ECO:0000269|PubMed:18171027, ECO:0000269|PubMed:19663506};
CC -!- ACTIVITY REGULATION: Inhibited by zinc ions (By similarity). Enzyme
CC purified in the absence of 1,10-phenanthroline contains on average 0.4
CC zinc atoms per subunit. Inhibited by 4-hydroxy-nonenal through the
CC formation of a covalent adduct with His-173. Competitively inhibited by
CC N(5)-iminopropyl-ornithine. {ECO:0000250, ECO:0000269|PubMed:18171027,
CC ECO:0000269|PubMed:19663506}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=69 uM for asymmetric dimethylarginine (ADMA)
CC {ECO:0000269|PubMed:18171027, ECO:0000269|PubMed:19663506};
CC KM=54 uM for monomethyl-L-arginine (MMA)
CC {ECO:0000269|PubMed:18171027, ECO:0000269|PubMed:19663506};
CC KM=3.1 uM for S-methyl-L-thiocitrulline {ECO:0000269|PubMed:18171027,
CC ECO:0000269|PubMed:19663506};
CC Vmax=356 nmol/min/mg enzyme with ADMA {ECO:0000269|PubMed:18171027,
CC ECO:0000269|PubMed:19663506};
CC Vmax=154 nmol/min/mg enzyme with NMA {ECO:0000269|PubMed:18171027,
CC ECO:0000269|PubMed:19663506};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:18171027,
CC ECO:0000269|PubMed:19663506};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19663506}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O94760-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94760-2; Sequence=VSP_043813;
CC -!- TISSUE SPECIFICITY: Detected in brain, liver, kidney and pancreas, and
CC at low levels in skeletal muscle. {ECO:0000269|PubMed:10493931}.
CC -!- SIMILARITY: Belongs to the DDAH family. {ECO:0000305}.
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DR EMBL; AB001915; BAA37117.1; -; mRNA.
DR EMBL; BX648145; CAI45988.1; -; mRNA.
DR EMBL; AC092807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL078459; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL360219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471097; EAW73199.1; -; Genomic_DNA.
DR EMBL; BC033680; AAH33680.1; -; mRNA.
DR EMBL; BC043235; AAH43235.2; -; mRNA.
DR CCDS; CCDS44170.1; -. [O94760-2]
DR CCDS; CCDS705.1; -. [O94760-1]
DR RefSeq; NP_001127917.1; NM_001134445.1. [O94760-2]
DR RefSeq; NP_036269.1; NM_012137.3. [O94760-1]
DR RefSeq; XP_005270767.1; XM_005270710.2. [O94760-2]
DR PDB; 2JAI; X-ray; 2.30 A; A/B=1-285.
DR PDB; 2JAJ; X-ray; 2.00 A; A/B=1-285.
DR PDB; 3I2E; X-ray; 2.03 A; A/B=1-285.
DR PDB; 3I4A; X-ray; 1.90 A; A/B=1-285.
DR PDB; 3P8E; X-ray; 2.49 A; A/B=1-285.
DR PDB; 3P8P; X-ray; 2.50 A; A/B=1-285.
DR PDB; 6DGE; X-ray; 1.91 A; A=1-285.
DR PDB; 6SZP; X-ray; 1.76 A; A=1-285.
DR PDB; 6SZQ; X-ray; 2.41 A; A/B/C/D/E/F=1-285.
DR PDBsum; 2JAI; -.
DR PDBsum; 2JAJ; -.
DR PDBsum; 3I2E; -.
DR PDBsum; 3I4A; -.
DR PDBsum; 3P8E; -.
DR PDBsum; 3P8P; -.
DR PDBsum; 6DGE; -.
DR PDBsum; 6SZP; -.
DR PDBsum; 6SZQ; -.
DR AlphaFoldDB; O94760; -.
DR SMR; O94760; -.
DR BioGRID; 117114; 44.
DR DIP; DIP-61582N; -.
DR IntAct; O94760; 14.
DR STRING; 9606.ENSP00000284031; -.
DR BindingDB; O94760; -.
DR ChEMBL; CHEMBL6036; -.
DR DrugBank; DB00155; Citrulline.
DR DrugBank; DB05351; Dexlansoprazole.
DR DrugBank; DB00736; Esomeprazole.
DR DrugBank; DB00213; Pantoprazole.
DR GuidetoPHARMACOLOGY; 1247; -.
DR iPTMnet; O94760; -.
DR PhosphoSitePlus; O94760; -.
DR SwissPalm; O94760; -.
DR BioMuta; DDAH1; -.
DR REPRODUCTION-2DPAGE; IPI00220342; -.
DR EPD; O94760; -.
DR jPOST; O94760; -.
DR MassIVE; O94760; -.
DR MaxQB; O94760; -.
DR PaxDb; O94760; -.
DR PeptideAtlas; O94760; -.
DR PRIDE; O94760; -.
DR ProteomicsDB; 50422; -. [O94760-1]
DR ProteomicsDB; 50423; -. [O94760-2]
DR Antibodypedia; 1588; 309 antibodies from 35 providers.
DR DNASU; 23576; -.
DR Ensembl; ENST00000284031.13; ENSP00000284031.8; ENSG00000153904.21. [O94760-1]
DR Ensembl; ENST00000426972.8; ENSP00000411189.4; ENSG00000153904.21. [O94760-2]
DR GeneID; 23576; -.
DR KEGG; hsa:23576; -.
DR MANE-Select; ENST00000284031.13; ENSP00000284031.8; NM_012137.4; NP_036269.1.
DR UCSC; uc001dlb.4; human. [O94760-1]
DR CTD; 23576; -.
DR DisGeNET; 23576; -.
DR GeneCards; DDAH1; -.
DR HGNC; HGNC:2715; DDAH1.
DR HPA; ENSG00000153904; Tissue enhanced (brain, kidney).
DR MIM; 604743; gene.
DR neXtProt; NX_O94760; -.
DR OpenTargets; ENSG00000153904; -.
DR PharmGKB; PA27185; -.
DR VEuPathDB; HostDB:ENSG00000153904; -.
DR eggNOG; ENOG502QWPA; Eukaryota.
DR GeneTree; ENSGT00940000157892; -.
DR HOGENOM; CLU_115111_0_0_1; -.
DR InParanoid; O94760; -.
DR OMA; HRYTHAI; -.
DR PhylomeDB; O94760; -.
DR TreeFam; TF314737; -.
DR BioCyc; MetaCyc:HS00016-MON; -.
DR BRENDA; 3.5.3.18; 2681.
DR PathwayCommons; O94760; -.
DR Reactome; R-HSA-203615; eNOS activation.
DR SignaLink; O94760; -.
DR BioGRID-ORCS; 23576; 16 hits in 1075 CRISPR screens.
DR ChiTaRS; DDAH1; human.
DR EvolutionaryTrace; O94760; -.
DR GenomeRNAi; 23576; -.
DR Pharos; O94760; Tchem.
DR PRO; PR:O94760; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O94760; protein.
DR Bgee; ENSG00000153904; Expressed in endothelial cell and 205 other tissues.
DR ExpressionAtlas; O94760; baseline and differential.
DR Genevisible; O94760; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016597; F:amino acid binding; IBA:GO_Central.
DR GO; GO:0003824; F:catalytic activity; TAS:ProtInc.
DR GO; GO:0016403; F:dimethylargininase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006527; P:arginine catabolic process; IDA:BHF-UCL.
DR GO; GO:0006525; P:arginine metabolic process; IBA:GO_Central.
DR GO; GO:0000052; P:citrulline metabolic process; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:1900038; P:negative regulation of cellular response to hypoxia; IDA:BHF-UCL.
DR GO; GO:0043116; P:negative regulation of vascular permeability; IDA:BHF-UCL.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; TAS:ProtInc.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0050999; P:regulation of nitric-oxide synthase activity; TAS:Reactome.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; ISS:BHF-UCL.
DR InterPro; IPR033199; DDAH.
DR InterPro; IPR033197; DDAH1.
DR PANTHER; PTHR12737; PTHR12737; 1.
DR PANTHER; PTHR12737:SF17; PTHR12737:SF17; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Hydrolase; Metal-binding; Reference proteome; S-nitrosylation; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9874257,
FT ECO:0007744|PubMed:19413330"
FT CHAIN 2..285
FT /note="N(G),N(G)-dimethylarginine dimethylaminohydrolase 1"
FT /id="PRO_0000171118"
FT ACT_SITE 173
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:19663506"
FT ACT_SITE 274
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:19663506"
FT BINDING 30
FT /ligand="substrate"
FT BINDING 73
FT /ligand="substrate"
FT BINDING 78..79
FT /ligand="substrate"
FT BINDING 98
FT /ligand="substrate"
FT BINDING 145
FT /ligand="substrate"
FT BINDING 268
FT /ligand="substrate"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:9874257,
FT ECO:0007744|PubMed:19413330"
FT MOD_RES 222
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P56965"
FT MOD_RES 274
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P56965"
FT VAR_SEQ 1..103
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_043813"
FT MUTAGEN 30
FT /note="L->A: Reduces enzyme activity and affinity for
FT asymmetric dimethylarginine about 12-fold."
FT /evidence="ECO:0000269|PubMed:19663506"
FT MUTAGEN 78
FT /note="E->A: Reduces enzyme activity about 1000-fold, and
FT affinity for asymmetric dimethylarginine about 100-fold."
FT /evidence="ECO:0000269|PubMed:19663506"
FT MUTAGEN 271
FT /note="L->G: Reduces enzyme activity about 10-fold, and
FT affinity for asymmetric dimethylarginine about 7-fold."
FT /evidence="ECO:0000269|PubMed:19663506"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:6SZP"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:6SZP"
FT HELIX 40..54
FT /evidence="ECO:0007829|PDB:6SZP"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:6SZP"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:6SZP"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:6SZP"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:6SZP"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:6SZP"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:6SZP"
FT HELIX 96..101
FT /evidence="ECO:0007829|PDB:6SZP"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:6SZP"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:6SZP"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:6SZP"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:6SZP"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:6SZP"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:6SZP"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:6SZP"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:6SZP"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:6SZP"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:6SZP"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:6SZP"
FT HELIX 192..204
FT /evidence="ECO:0007829|PDB:6SZP"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:6SZP"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:6SZP"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:6SZP"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:6SZP"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:6SZP"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:6SZP"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:6SZP"
FT HELIX 243..250
FT /evidence="ECO:0007829|PDB:6SZP"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:6SZP"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:6SZP"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:6SZP"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:6SZP"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:6SZP"
SQ SEQUENCE 285 AA; 31122 MW; CD8875DF267EF39B CRC64;
MAGLGHPAAF GRATHAVVRA LPESLGQHAL RSAKGEEVDV ARAERQHQLY VGVLGSKLGL
QVVELPADES LPDCVFVEDV AVVCEETALI TRPGAPSRRK EVDMMKEALE KLQLNIVEMK
DENATLDGGD VLFTGREFFV GLSKRTNQRG AEILADTFKD YAVSTVPVAD GLHLKSFCSM
AGPNLIAIGS SESAQKALKI MQQMSDHRYD KLTVPDDIAA NCIYLNIPNK GHVLLHRTPE
EYPESAKVYE KLKDHMLIPV SMSELEKVDG LLTCCSVLIN KKVDS
