ID   ASTB_PARXL              Reviewed;         446 AA.
AC   Q141D2;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Bxeno_A1519;
GN   ORFNames=Bxe_A2919;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000270; ABE30057.1; -; Genomic_DNA.
DR   RefSeq; WP_011487767.1; NZ_CP008760.1.
DR   AlphaFoldDB; Q141D2; -.
DR   SMR; Q141D2; -.
DR   STRING; 266265.Bxe_A2919; -.
DR   EnsemblBacteria; ABE30057; ABE30057; Bxe_A2919.
DR   KEGG; bxb:DR64_601; -.
DR   KEGG; bxe:Bxe_A2919; -.
DR   PATRIC; fig|266265.5.peg.1570; -.
DR   eggNOG; COG3724; Bacteria.
DR   OMA; TLNDWVD; -.
DR   OrthoDB; 567590at2; -.
DR   UniPathway; UPA00185; UER00280.
DR   Proteomes; UP000001817; 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; -; 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..446
FT                   /note="N-succinylarginine dihydrolase"
FT                   /id="PRO_0000262344"
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;  48896 MW;  3FF0ECB529441E9A CRC64;
     MQATEANFDG LVGPTHNYAG LSFGNVASQN NEKSVANPKA AAKQGLRKMK QLADLGFHQG
     VLPPQERPSM RLLRELGFSG DDATVIARVA RDAPELLAAA SSASAMWTAN AATVSPSADT
     NDGRVHFTPA NLCSKLHRAI EHESTRRTLR TMFNDTDRFV VHEALPGTPA LGDEGAANHT
     RFCEEYGARG VEFFVYGRSE YRRGPEPKRF PARQSFEASR AVAHRHGLAD EATVYAQQNP
     DVIDAGVFHN DVIAVGNRNT LFCHQFAFVE PNAVYDELRA KLSGLKAAFN VIEVPDAQVS
     VADAVSSYLF NSQLLTRPDG KQVLVVPQEC RENPRVAAYL DDLTSRTGPI DDVLVFDLRE
     SMKNGGGPAC LRLRVVLDDA ERAAVTPGVW IDDTLFGRLD AWIEKHYRDR LAPADLTDPH
     LLAESRTALD ELTQILGLGS LYDFQR