DDAH_MYCTU
ID DDAH_MYCTU Reviewed; 302 AA.
AC P71889; F2GIS4; I6YD48; Q7D7B6;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 128.
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 OrderedLocusNames=Rv2323c {ECO:0000312|EMBL:CCP45110.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
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; AL123456; CCP45110.1; -; Genomic_DNA.
DR RefSeq; NP_216839.1; NC_000962.3.
DR RefSeq; WP_003411960.1; NC_000962.3.
DR AlphaFoldDB; P71889; -.
DR SMR; P71889; -.
DR STRING; 83332.Rv2323c; -.
DR PaxDb; P71889; -.
DR DNASU; 885480; -.
DR GeneID; 885480; -.
DR KEGG; mtu:Rv2323c; -.
DR PATRIC; fig|83332.111.peg.2587; -.
DR TubercuList; Rv2323c; -.
DR eggNOG; COG1834; Bacteria.
DR OMA; GAKCCTL; -.
DR PhylomeDB; P71889; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016403; F:dimethylargininase activity; IDA:MTBBASE.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..302
FT /note="N(G),N(G)-dimethylarginine dimethylaminohydrolase"
FT /id="PRO_0000443949"
FT ACT_SITE 201
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9I4E3"
FT ACT_SITE 295
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9I4E3"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9I4E3"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9I4E3"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9I4E3"
SQ SEQUENCE 302 AA; 32960 MW; 5AE40058ACDE55E2 CRC64;
MENTQRPSFD CEIRAKYRWF MTDSYVAAAR LGSPARRTPR TRRYAMTPPA FFAVAYAINP
WMDVTAPVDV QVAQAQWEHL HQTYLRLGHS VDLIEPISGL PDMVYTANGG FIAHDIAVVA
RFRFPERAGE SRAYASWMSS VGYRPVTTRH VNEGQGDLLM VGERVLAGYG FRTDQRAHAE
IAAVLGLPVV SLELVDPRFY HLDTALAVLD DHTIAYYPPA FSTAAQEQLS ALFPDAIVVG
SADAFVFGLN AVSDGLNVVL PVAAMGFAAQ LRAAGFEPVG VDLSELLKGG GSVKCCTLEI
HP