ASTB_BURM9
ID ASTB_BURM9 Reviewed; 446 AA.
AC A2SA47;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 66.
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};
GN OrderedLocusNames=BMA10229_A2870;
OS Burkholderia mallei (strain NCTC 10229).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=412022;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 10229;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
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; CP000546; ABN03653.1; -; Genomic_DNA.
DR RefSeq; WP_004192611.1; NC_008836.1.
DR AlphaFoldDB; A2SA47; -.
DR SMR; A2SA47; -.
DR EnsemblBacteria; ABN03653; ABN03653; BMA10229_A2870.
DR GeneID; 56596294; -.
DR KEGG; bml:BMA10229_A2870; -.
DR HOGENOM; CLU_053835_0_0_4; -.
DR OMA; TLNDWVD; -.
DR UniPathway; UPA00185; UER00280.
DR Proteomes; UP000002283; Chromosome I.
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.
FT CHAIN 1..446
FT /note="N-succinylarginine dihydrolase"
FT /id="PRO_1000065717"
FT ACT_SITE 174
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT ACT_SITE 249
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT ACT_SITE 370
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 213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
SQ SEQUENCE 446 AA; 48138 MW; 934449B79BB55B2F CRC64;
MNAKEANFDG LVGPTHNYAG LSFGNVASLS NEKSDANPKA AAKQGLRKMK QLADLGFAQG
VLPPQERPSL RLLRELGFSG KDADVIAKAA RQAPELLAAA SSASAMWTAN AATVSPSADT
SDARVHFTPA NLCSKLHRAI EHESTRRTLA AIFADEARFA VHDALPGTPA LGDEGAANHT
RFCAEYGAPG VEFFVYGRAE YRRGPEPTRF PARQTFEASR AVAHRHGLRE EATIYAQQRP
DVIDAGVFHN DVIAVGNRDT LFCHEHAFVD RQAVYDALAA SLGALGAQLN VIEVPDRAVS
VADAVGSYLF NSQLLAREDG TQMLVVPQEC RENANVAAYL DALVAGNGPI RDVRVFDLRE
SMKNGGGPAC LRLRVVLNDA ERAAVKPNVW IGDALFASLD AWIDKHYRDR LSPVDLADPA
LLDESRTALD ELTQILGLGS LYDFQR
