DAUB_PSEAE
ID DAUB_PSEAE Reviewed; 315 AA.
AC Q9HXE4;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=NAD(P)H-dependent anabolic L-arginine dehydrogenase DauB {ECO:0000303|PubMed:19139398};
DE EC=1.4.1.25 {ECO:0000269|PubMed:19139398};
GN Name=dauB {ECO:0000303|PubMed:19139398}; OrderedLocusNames=PA3862;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=19139398; DOI=10.1073/pnas.0808269106;
RA Li C., Lu C.D.;
RT "Arginine racemization by coupled catabolic and anabolic dehydrogenases.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:906-911(2009).
RN [3]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=19850617; DOI=10.1099/mic.0.033282-0;
RA Li C., Yao X., Lu C.D.;
RT "Regulation of the dauBAR operon and characterization of D-amino acid
RT dehydrogenase DauA in arginine and lysine catabolism of Pseudomonas
RT aeruginosa PAO1.";
RL Microbiology 156:60-71(2010).
CC -!- FUNCTION: Involved in the anabolism of D-lysine and D-arginine. Under
CC aerobic conditions, the arginine succinyltransferase (AST) and arginine
CC transaminase (ATA) pathways are 2 major routes for L-arginine
CC utilization as the sole source of carbon and nitrogen. The D-to-L
CC racemization of arginine by DauA and DauB is necessary, before to be
CC channeled into the AST and/or ATA pathways. DauB catalyzes the
CC synthesis of L-arginine from 2-ketoarginine (2-KA) and ammonium.
CC {ECO:0000269|PubMed:19139398, ECO:0000269|PubMed:19850617}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-arginine + NAD(+) = 5-guanidino-2-oxopentanoate + H(+)
CC + NADH + NH4(+); Xref=Rhea:RHEA:47632, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58489; EC=1.4.1.25;
CC Evidence={ECO:0000269|PubMed:19139398};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-arginine + NADP(+) = 5-guanidino-2-oxopentanoate +
CC H(+) + NADPH + NH4(+); Xref=Rhea:RHEA:47636, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58489; EC=1.4.1.25;
CC Evidence={ECO:0000269|PubMed:19139398};
CC -!- INDUCTION: Induced by growth on D-arginine and D-lysine. Repressed by
CC DauR (PubMed:19139398). ArgR could be a transcriptional activator of
CC the dauBAR operon in response to the presence of L-Arg
CC (PubMed:19850617). {ECO:0000269|PubMed:19139398,
CC ECO:0000269|PubMed:19850617}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow similarly to the
CC wild-type on D-Arg or D-Lys as sole nitrogen source, but are unable to
CC grow on D-Arg as sole carbon source. {ECO:0000269|PubMed:19139398,
CC ECO:0000269|PubMed:19850617}.
CC -!- SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG07249.1; -; Genomic_DNA.
DR PIR; D83163; D83163.
DR RefSeq; NP_252551.1; NC_002516.2.
DR RefSeq; WP_003113781.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; Q9HXE4; -.
DR SMR; Q9HXE4; -.
DR STRING; 287.DR97_4004; -.
DR PaxDb; Q9HXE4; -.
DR PRIDE; Q9HXE4; -.
DR EnsemblBacteria; AAG07249; AAG07249; PA3862.
DR GeneID; 879805; -.
DR KEGG; pae:PA3862; -.
DR PATRIC; fig|208964.12.peg.4044; -.
DR PseudoCAP; PA3862; -.
DR HOGENOM; CLU_042088_2_1_6; -.
DR InParanoid; Q9HXE4; -.
DR OMA; LLMSMQT; -.
DR PhylomeDB; Q9HXE4; -.
DR BioCyc; MetaCyc:MON-15372; -.
DR BioCyc; PAER208964:G1FZ6-3933-MON; -.
DR BRENDA; 1.4.1.25; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0006527; P:arginine catabolic process; IMP:UniProtKB.
DR GO; GO:0006525; P:arginine metabolic process; IMP:UniProtKB.
DR Gene3D; 3.30.1780.10; -; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003462; ODC_Mu_crystall.
DR InterPro; IPR023401; ODC_N.
DR PANTHER; PTHR13812; PTHR13812; 1.
DR Pfam; PF02423; OCD_Mu_crystall; 1.
DR PIRSF; PIRSF001439; CryM; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..315
FT /note="NAD(P)H-dependent anabolic L-arginine dehydrogenase
FT DauB"
FT /id="PRO_0000433132"
SQ SEQUENCE 315 AA; 33945 MW; AF7B52F8F3484715 CRC64;
MSAATPLIVQ QAEAEQLLAR IDVLQAMRQL FLDLAAGQAL QPAQQLVEFP AGRGDFINYL
GVLAQEQVYG VKTSPYIVRE QGPLVTAWTL LMSMQTGQPL LLCDAARLTT ARTAATTAVA
VDALAPAEAC RLALIGSGPV AHAHLQYVKG LRDWQGVRVH SPCLDERRLQ SLRAIDPRAE
AAGSLEEALD EADVILLCTS SARAVIDPRQ LKRPALVTSI STNAPRAHEV PAESLAAMDV
YCDYRHTTPG SAGEMLIAAE QHGWSPEAIR GDLAELLSAQ APRPEYRRPA FFRSIGLGLE
DVALANALYR LRQAG
