ID   ASTB_BURCM              Reviewed;         446 AA.
AC   Q0BGU9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 84.
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=Bamb_1065;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000440; ABI86624.1; -; Genomic_DNA.
DR   RefSeq; WP_011656402.1; NZ_CP009798.1.
DR   AlphaFoldDB; Q0BGU9; -.
DR   SMR; Q0BGU9; -.
DR   GeneID; 69544778; -.
DR   KEGG; bam:Bamb_1065; -.
DR   PATRIC; fig|339670.21.peg.503; -.
DR   eggNOG; COG3724; Bacteria.
DR   UniPathway; UPA00185; UER00280.
DR   Proteomes; UP000000662; Chromosome 1.
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; Succinylarginine dihydrolase; 1.
DR   HAMAP; MF_01172; AstB; 1.
DR   InterPro; IPR037031; AstB_sf.
DR   InterPro; IPR007079; SuccinylArg_d-Hdrlase_AstB.
DR   NCBIfam; TIGR03241; arg_catab_astB; 1.
DR   PANTHER; PTHR30420; N-SUCCINYLARGININE DIHYDROLASE; 1.
DR   PANTHER; PTHR30420:SF2; N-SUCCINYLARGININE DIHYDROLASE; 1.
DR   Pfam; PF04996; AstB; 1.
DR   SUPFAM; SSF55909; Pentein; 1.
PE   3: Inferred from homology;
KW   Arginine metabolism; Hydrolase.
FT   CHAIN           1..446
FT                   /note="N-succinylarginine dihydrolase"
FT                   /id="PRO_1000065715"
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;  48330 MW;  9C8CAD015D021187 CRC64;
     MNAQEANFDG LVGPTHNYAG LSFGNVASLN NEKSAANPKA AAKQGLRKMK QLADLGFAQG
     VLPPQERPSL RLLRELGFSG KDADVIAKAA KQAPELLAAA SSASAMWTAN AATVSPSADT
     GDGRVHFTPA NLCSKLHRAI EHDATRRTLS TLFADPAHFA VHEALTGTPA LGDEGAANHT
     RFCAEYGKPG VEFFVYGRAE YRRGPEPKRF PARQTFEASR AVAQRHGLDE TATVYAQQDP
     DVIDAGVFHN DVISVGNRDT LFTHERAFVN KQAIYDTLTA TLDARGARLN VIEVPDAAVS
     VNDAVTSYLF NSQLLSRADG SQVLVVPQEC RENAKVAAYL DELAAGNGPI RDVLVFDLRE
     SMKNGGGPAC LRLRVVLNDA ERAAVTSNVW MNDTLFASLD AWIEKHYRDR LAPEDLADPT
     LLDESRTALD ELTQILRVGS LYDFQR
//