ID   DDAH_STRCO              Reviewed;         258 AA.
AC   Q9X7M4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=N(G),N(G)-dimethylarginine dimethylaminohydrolase {ECO:0000305};
DE            Short=DDAH {ECO:0000303|PubMed:10510241};
DE            Short=Dimethylarginine dimethylaminohydrolase {ECO:0000303|PubMed:10510241};
DE            EC=3.5.3.18 {ECO:0000269|PubMed:10510241};
DE   AltName: Full=Dimethylargininase {ECO:0000305};
GN   Name=ddaH; OrderedLocusNames=SCO6718; ORFNames=SC5F2A.01c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=10510241; DOI=10.1046/j.1365-2958.1999.01580.x;
RA   Santa Maria J., Vallance P., Charles I.G., Leiper J.M.;
RT   "Identification of microbial dimethylarginine dimethylaminohydrolase
RT   enzymes.";
RL   Mol. Microbiol. 33:1278-1279(1999).
CC   -!- FUNCTION: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-
CC       monomethyl-L-arginine (MMA). {ECO:0000269|PubMed:10510241}.
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:10510241};
CC   -!- SIMILARITY: Belongs to the DDAH family. {ECO:0000305}.
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DR   EMBL; AL939129; CAB40668.1; -; Genomic_DNA.
DR   PIR; T35243; T35243.
DR   RefSeq; NP_630791.1; NC_003888.3.
DR   RefSeq; WP_003972278.1; NZ_VNID01000002.1.
DR   AlphaFoldDB; Q9X7M4; -.
DR   SMR; Q9X7M4; -.
DR   STRING; 100226.SCO6718; -.
DR   GeneID; 1102157; -.
DR   KEGG; sco:SCO6718; -.
DR   PATRIC; fig|100226.15.peg.6825; -.
DR   eggNOG; COG1834; Bacteria.
DR   HOGENOM; CLU_067923_1_0_11; -.
DR   InParanoid; Q9X7M4; -.
DR   OMA; HRYTHAI; -.
DR   PhylomeDB; Q9X7M4; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0016597; F:amino acid binding; IBA:GO_Central.
DR   GO; GO:0016403; F:dimethylargininase activity; IBA:GO_Central.
DR   GO; GO:0006525; P:arginine metabolic process; IBA:GO_Central.
DR   GO; GO:0000052; P:citrulline metabolic process; IBA:GO_Central.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR033199; DDAH.
DR   PANTHER; PTHR12737; PTHR12737; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..258
FT                   /note="N(G),N(G)-dimethylarginine dimethylaminohydrolase"
FT                   /id="PRO_0000171123"
FT   ACT_SITE        163
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I4E3"
FT   ACT_SITE        248
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I4E3"
FT   BINDING         19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I4E3"
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I4E3"
FT   BINDING         67..68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I4E3"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I4E3"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I4E3"
SQ   SEQUENCE   258 AA;  27571 MW;  7C0DBD329B094DBD CRC64;
     MPSKKALVRR PSPRLAEGLV THVEREKVDH GLALEQWDAY VEALGAHGWE TLEVDPADDC
     PDSVFVEDAV VVFRNVALIT RPGAESRRAE TAGVEEAVAR LGCSVNWVWE PGTLDGGDVL
     KIGDTIYVGR GGRTNAAGVQ QLRAAFEPLG ARVVAVPVSK VLHLKSAVTA LPDGTVIGHI
     PLTDVPSLFP RFLPVPEESG AHVVLLGGSR LLMAASAPKT AELLADLGHE PVLVDIGEFE
     KLEGCVTCLS VRLRELYD