ARUI_PSEAE
ID ARUI_PSEAE Reviewed; 559 AA.
AC Q9HUI8;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Probable 2-ketoarginine decarboxylase AruI;
DE EC=4.1.1.75;
DE AltName: Full=2-oxo-5-guanidinopentanoate decarboxylase;
DE AltName: Full=5-guanidino-2-oxopentanoate decarboxylase;
GN Name=aruI; OrderedLocusNames=PA4977;
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 IN ARGININE DEGRADATION, PATHWAY, INDUCTION, AND GENE NAME.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=17416670; DOI=10.1128/jb.00261-07;
RA Yang Z., Lu C.D.;
RT "Functional genomics enables identification of genes of the arginine
RT transaminase pathway in Pseudomonas aeruginosa.";
RL J. Bacteriol. 189:3945-3953(2007).
CC -!- FUNCTION: Catalyzes the decarboxylation of 2-ketoarginine, leading to
CC the formation of 4-guanidinobutyraldehyde.
CC {ECO:0000305|PubMed:17416670}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-guanidino-2-oxopentanoate + H(+) = 4-guanidinobutanal + CO2;
CC Xref=Rhea:RHEA:11340, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57854, ChEBI:CHEBI:58489; EC=4.1.1.75;
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation.
CC {ECO:0000269|PubMed:17416670}.
CC -!- INDUCTION: Induced by L-arginine in the absence of ArgR, via the
CC AruR/AruS two-component regulatory system.
CC {ECO:0000269|PubMed:17416670}.
CC -!- SIMILARITY: Belongs to the TPP enzyme 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; AAG08362.1; -; Genomic_DNA.
DR PIR; G83024; G83024.
DR RefSeq; NP_253664.1; NC_002516.2.
DR RefSeq; WP_010895690.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; Q9HUI8; -.
DR SMR; Q9HUI8; -.
DR STRING; 287.DR97_2330; -.
DR PaxDb; Q9HUI8; -.
DR EnsemblBacteria; AAG08362; AAG08362; PA4977.
DR GeneID; 880189; -.
DR KEGG; pae:PA4977; -.
DR PATRIC; fig|208964.12.peg.5213; -.
DR PseudoCAP; PA4977; -.
DR HOGENOM; CLU_013748_3_1_6; -.
DR InParanoid; Q9HUI8; -.
DR OMA; FNDFYPS; -.
DR PhylomeDB; Q9HUI8; -.
DR BioCyc; PAER208964:G1FZ6-5093-MON; -.
DR UniPathway; UPA00073; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005948; C:acetolactate synthase complex; IBA:GO_Central.
DR GO; GO:0047435; F:5-guanidino-2-oxopentanoate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0003984; F:acetolactate synthase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0019545; P:arginine catabolic process to succinate; IMP:UniProtKB.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR PANTHER; PTHR18968; PTHR18968; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 1: Evidence at protein level;
KW Arginine metabolism; Lyase; Reference proteome; Thiamine pyrophosphate.
FT CHAIN 1..559
FT /note="Probable 2-ketoarginine decarboxylase AruI"
FT /id="PRO_0000418391"
FT BINDING 76
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
SQ SEQUENCE 559 AA; 59402 MW; 07E9794E51F2B266 CRC64;
MGARALRRER RLRWSPNWTR ILPMQPQKTL TAGQALVRLL ANYGVDTVFG IPGVHTLELY
RGLPGSGIRH VLTRHEQGAG FMADGYARVS GKPGVCFVIT GPGVTNVATA IGQAYADSVP
LLVISSVNHS ASLGKGWGCL HETQDQRAMT APITAFSALA LSPEQLPELI ARAYAVFDSE
RPRPVHISIP LDVLAAPVAH DWSAAVARRP GRGVPCSEAL RAAAERLAAA RRPMLIAGGG
ALAAGEALAA LSERLAAPLF TSVAGKGLLP PDAPLNAGAS LCVAPGWEMI AEADLVLAVG
TEMADTDFWR ERLPLSGELI RVDIDPRKFN DFYPSAVALR GDARQTLEAL LVRLPQEARD
SAPAAARVAR LRAEIRAAHA PLQALHQAIL DRIAAALPAD AFVSTDMTQL AYTGNYAFAS
RAPRSWLHPT GYGTLGYGLP AGIGAKLGAP QRPGLVLVGD GGFLYTAQEL ATASEELDSP
LVVLLWNNDA LGQIRDDMLG LDIEPVGVLP RNPDFALLGR AYGCAVRQPQ DLDELERDLR
AGFGQSGVTL IELRHACAR
