ASTB_PSEAE
ID ASTB_PSEAE Reviewed; 448 AA.
AC O50175;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=N-succinylarginine dihydrolase {ECO:0000255|HAMAP-Rule:MF_01172};
DE EC=3.5.3.23 {ECO:0000255|HAMAP-Rule:MF_01172};
GN Name=astB {ECO:0000255|HAMAP-Rule:MF_01172}; Synonyms=aruB;
GN OrderedLocusNames=PA0899;
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 [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9393691; DOI=10.1128/jb.179.23.7280-7290.1997;
RA Itoh Y.;
RT "Cloning and characterization of the aru genes encoding enzymes of the
RT catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa.";
RL J. Bacteriol. 179:7280-7290(1997).
RN [2]
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).
CC -!- FUNCTION: Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-
CC succinylornithine, ammonia and CO(2).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 H2O + N(2)-succinyl-L-arginine = CO2 + N(2)-
CC succinyl-L-ornithine + 2 NH4(+); Xref=Rhea:RHEA:19533,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:58241, ChEBI:CHEBI:58514; EC=3.5.3.23;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01172};
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC pathway; L-glutamate and succinate from L-arginine: step 2/5.
CC {ECO:0000255|HAMAP-Rule:MF_01172}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01172}.
CC -!- SIMILARITY: Belongs to the succinylarginine dihydrolase family.
CC {ECO:0000255|HAMAP-Rule:MF_01172}.
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DR EMBL; AF011922; AAC46013.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04288.1; -; Genomic_DNA.
DR PIR; D83533; D83533.
DR RefSeq; NP_249590.1; NC_002516.2.
DR RefSeq; WP_003085956.1; NZ_QZGE01000007.1.
DR AlphaFoldDB; O50175; -.
DR SMR; O50175; -.
DR STRING; 287.DR97_1044; -.
DR PaxDb; O50175; -.
DR PRIDE; O50175; -.
DR EnsemblBacteria; AAG04288; AAG04288; PA0899.
DR GeneID; 878588; -.
DR KEGG; pae:PA0899; -.
DR PATRIC; fig|208964.12.peg.934; -.
DR PseudoCAP; PA0899; -.
DR HOGENOM; CLU_053835_0_0_6; -.
DR InParanoid; O50175; -.
DR OMA; IAPTNCQ; -.
DR PhylomeDB; O50175; -.
DR BioCyc; PAER208964:G1FZ6-915-MON; -.
DR UniPathway; UPA00185; UER00280.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0009015; F:N-succinylarginine dihydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006527; P:arginine catabolic process; IDA:PseudoCAP.
DR GO; GO:0019544; P:arginine catabolic process to glutamate; IEA:UniProtKB-UniRule.
DR GO; GO:0019545; P:arginine catabolic process to succinate; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.75.10.20; -; 1.
DR HAMAP; MF_01172; AstB; 1.
DR InterPro; IPR037031; AstB_sf.
DR InterPro; IPR007079; SuccinylArg_d-Hdrlase_AstB.
DR Pfam; PF04996; AstB; 1.
DR TIGRFAMs; TIGR03241; arg_catab_astB; 1.
PE 3: Inferred from homology;
KW Arginine metabolism; Hydrolase; Reference proteome.
FT CHAIN 1..448
FT /note="N-succinylarginine dihydrolase"
FT /id="PRO_0000064716"
FT ACT_SITE 174
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT ACT_SITE 250
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT ACT_SITE 371
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 19..28
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 137..138
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
SQ SEQUENCE 448 AA; 48875 MW; 39F9F379CCC16196 CRC64;
MNAHEVNFDG LVGPTHNYGG LSYGNVASQS NSQAVSNPKE AAKQGLAKMK ALMEMGFKQG
VLAPQARPDT AALRSLGFSG SDEEVIRRAA KEAMPLLAAC SSASSMWTAN AATVSPSADT
ADGRVHFTAA NLNCKFHRSI EHPTTSRVLA AMFNDERHFA HHAALPAVSQ FGDEGAANHT
RFCKDYGDAG VEFFVFGRSA FDSRFPAPQR YPARQTLEAC QAVARLHGLS EAGVVYAQQN
PAVIDQGVFH NDVISVGNGE VLFHHEDAFL DTEKVLAELH DKLGRRGGRF RAICVPRDQV
AVEDAVKSYL FNSQLLSKAD GSMLLVVPEE CRNNPRVWNY LDQLTGDDGP IREVKVFDLK
QSMQNGGGPA CLRLRVALQE RELAAVNPGV IMSAGLYDTL VAWVDRHYRD RLSETDLADP
QLLLECRTAL DELTQILKLG SVYSFQLD
