ASTB_PSEFS
ID ASTB_PSEFS Reviewed; 448 AA.
AC C3JXY6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 86.
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}; OrderedLocusNames=PFLU_4753;
OS Pseudomonas fluorescens (strain SBW25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216595;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBW25;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
CC -!- FUNCTION: Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-
CC succinylornithine, ammonia and CO(2). {ECO:0000255|HAMAP-
CC Rule:MF_01172}.
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; AM181176; CAY51577.1; -; Genomic_DNA.
DR RefSeq; WP_015885472.1; NC_012660.1.
DR AlphaFoldDB; C3JXY6; -.
DR SMR; C3JXY6; -.
DR STRING; 294.SRM1_04228; -.
DR PRIDE; C3JXY6; -.
DR EnsemblBacteria; CAY51577; CAY51577; PFLU_4753.
DR KEGG; pfs:PFLU_4753; -.
DR PATRIC; fig|216595.4.peg.4887; -.
DR eggNOG; COG3724; Bacteria.
DR HOGENOM; CLU_053835_0_0_6; -.
DR OMA; IAPTNCQ; -.
DR OrthoDB; 567590at2; -.
DR UniPathway; UPA00185; UER00280.
DR Proteomes; UP000002332; Chromosome.
DR GO; GO:0009015; F:N-succinylarginine dihydrolase activity; IEA:UniProtKB-UniRule.
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_1000213740"
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; 48772 MW; 9D7EE5AB58D5CFC8 CRC64;
MKSYEVNFDG LVGPTHNYGG LSYGNVASQS NSQQSSNPKE AALQGLQKMK ALMDMGFVQG
VLAPQERPDV AALRNLGFSG TDAQVIQQAA KHAMPLLVAS CSASSMWVAN AATVSPSADT
ADGRVHFTAA NLNCKYHRSI EHPTTSRVLG AMFADQKHFA HHAALPAVAQ FGDEGAANHT
RFCRDYGEAG VEFFVYGRSA FDTRYPAPQK YPARQTLEAS QAVARLHGLQ DDGVVYAQQN
PAVIDAGVFH NDVIAVGNGE VLFYHEDAFL NTEQMLGELH GKLGKLGGHF QSVCVPRAQV
SVEDAVRSYL FNSQLLSRAD GSMLLIVPEE CRANERVWQY LQGLTASGGL IREVKVFDLK
QSMQNGGGPA CLRLRVALNE TELAAVNPGV IMTAPLYDTL TQWVDKHYRD SLRETDLADP
QLLLECRTAL DELTQILKLG SVYPFQIN
