ID   ASTB_PSET1              Reviewed;         448 AA.
AC   Q3ID31;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=PSHAb0177;
OS   Pseudoalteromonas translucida (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA   Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT   Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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; CR954247; CAI89223.1; -; Genomic_DNA.
DR   RefSeq; WP_011329814.1; NC_007482.1.
DR   AlphaFoldDB; Q3ID31; -.
DR   SMR; Q3ID31; -.
DR   STRING; 326442.PSHAb0177; -.
DR   EnsemblBacteria; CAI89223; CAI89223; PSHAb0177.
DR   KEGG; pha:PSHAb0177; -.
DR   PATRIC; fig|326442.8.peg.3090; -.
DR   eggNOG; COG3724; Bacteria.
DR   HOGENOM; CLU_053835_0_0_6; -.
DR   OMA; IAPTNCQ; -.
DR   OrthoDB; 567590at2; -.
DR   BioCyc; PHAL326442:PSHA_RS15720-MON; -.
DR   UniPathway; UPA00185; UER00280.
DR   Proteomes; UP000006843; Chromosome II.
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_0000262364"
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        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         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         364
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
SQ   SEQUENCE   448 AA;  49413 MW;  1B310DDD6A4DC06C CRC64;
     MPALEVNFDG LVGPTHNYAG LSYGNVASLN NAASFSNPQE AVLQGLEKMK AMHDKGLTQG
     VFAPHARPDL NILRRLGFSG NDAQIINKAF NADPILLRAC YSASAMWTAN AATVSPSPDT
     TDGKVHFTAA NLNNKFHRSL EPATTTRLLK AMFNNQNHFA HHTHLPDQGF FGDEGAANHT
     RFCDSHGEQG LEMFVFGASA FNSHLPKPVK FPARQTLEAS EAICRLHNLK DTSQILLQQN
     PDVIDQGVFH NDVIAVGNAN VLLCHQQAFL NQQQALQDIR EAYVGNKQFY IIEVPTSKVT
     IQDAVSSYLF NSQLVSLSDG SMLLVAPKEC QRNSAVNDYI EEMIMADNPI NQVRFFDLRQ
     SMQNGGGPAC LRLRVALNEQ ELAAVNPDVI LTDTKYTQLC NWAQRNYRDQ LGAKDFADPA
     LLSESYQALD ELTQLLNLGS VYDFQLEG