ID   ASTB_MARN8              Reviewed;         446 AA.
AC   A1U5W7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, 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=Maqu_3315;
OS   Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter
OS   aquaeolei).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Marinobacteraceae; Marinobacter.
OX   NCBI_TaxID=351348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700491 / DSM 11845 / VT8;
RX   PubMed=21335390; DOI=10.1128/aem.01866-10;
RA   Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A.,
RA   Edwards K.J.;
RT   "Genomic potential of Marinobacter aquaeolei, a biogeochemical
RT   'opportunitroph'.";
RL   Appl. Environ. Microbiol. 77:2763-2771(2011).
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; CP000514; ABM20386.1; -; Genomic_DNA.
DR   RefSeq; WP_011786727.1; NC_008740.1.
DR   AlphaFoldDB; A1U5W7; -.
DR   SMR; A1U5W7; -.
DR   STRING; 351348.Maqu_3315; -.
DR   EnsemblBacteria; ABM20386; ABM20386; Maqu_3315.
DR   KEGG; maq:Maqu_3315; -.
DR   eggNOG; COG3724; Bacteria.
DR   HOGENOM; CLU_053835_0_0_6; -.
DR   OMA; IAPTNCQ; -.
DR   OrthoDB; 567590at2; -.
DR   UniPathway; UPA00185; UER00280.
DR   Proteomes; UP000000998; 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.
FT   CHAIN           1..446
FT                   /note="N-succinylarginine dihydrolase"
FT                   /id="PRO_1000213739"
FT   ACT_SITE        176
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT   ACT_SITE        252
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         21..30
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT   BINDING         139..140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT   BINDING         216
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT   BINDING         254
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;  48399 MW;  6D487CB7F5D96BF4 CRC64;
     MVKHAVEANF DGLVGPTHNY AGLSWGNVAS KSNVNAVANP REAALQGLAK MKRLADRGYV
     QGILPPHERP HIPTLRALGF EGNERQILEA VAKADPTILA AVSSASCMWT ANAATVSPSA
     DTADHRVHFT PANLSAKFHR SIEHQVTGRS LKAIFGDESY FAHHPALPSV SHFGDEGAAN
     HTRLCSRYGE PGVELFVYGQ VAFNESAPAP GKYPARQTLE ASRAIARLHG LTDRHAVFAQ
     QNPAAIDAGV FHNDVIAVGN GNCLFYHEQA FLDEARVLAD IQERLTGAEL EAVRVSSTQV
     PIEDAVASYL FNSQLLNTAD GMLLAVPGEC REVASVSRYL DELVKADTPI TAVEVFDVKQ
     SMRNGGGPAC LRLRVVLNDD ELHAINRGVI LTDALYERLT SWVEAHYRDQ LSQQDLADPM
     LLEEVRKALD ELTGILGLGS IYDFQL