ASTB_SHESH
ID ASTB_SHESH Reviewed; 445 AA.
AC A8FX76;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Ssed_2842;
OS Shewanella sediminis (strain HAW-EB3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=425104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB3;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella sediminis HAW-EB3.";
RL Submitted (AUG-2007) 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; CP000821; ABV37449.1; -; Genomic_DNA.
DR RefSeq; WP_012143179.1; NC_009831.1.
DR AlphaFoldDB; A8FX76; -.
DR SMR; A8FX76; -.
DR STRING; 425104.Ssed_2842; -.
DR PRIDE; A8FX76; -.
DR EnsemblBacteria; ABV37449; ABV37449; Ssed_2842.
DR KEGG; sse:Ssed_2842; -.
DR eggNOG; COG3724; Bacteria.
DR HOGENOM; CLU_053835_0_0_6; -.
DR OMA; IAPTNCQ; -.
DR OrthoDB; 567590at2; -.
DR UniPathway; UPA00185; UER00280.
DR Proteomes; UP000002015; 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..445
FT /note="N-succinylarginine dihydrolase"
FT /id="PRO_1000085400"
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 369
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 363
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
SQ SEQUENCE 445 AA; 48866 MW; 7F17690672352145 CRC64;
MKHFEANFDG LVGPTHNYAG LSFGNVASLN NAAATSNPRA AAKQGLKKAK ALADMGMVQG
MLAPQERPDL HTLRRIGFSG TDAEILNKAA KEAPALLRAC CSASSMWTAN AATVSPSADT
HDGKLHFTPA NLVDKLHRSI EPETTGNILA ATFNNSRHFA HHQHLPEHSS FGDEGAANHT
RLCKDYGNAG VELFVYGQEA TNPAAPKPSK FPARQTLEAS QAIARLHQLD DENTVFISQN
PDVIDQGVFH NDVIAVGNQN VLFYHEQAFL DTKRKLDEIK RKFGDSELHF IEVPTSRVAI
QDAVKSYLFN TQIITLPSGE MAIIAPTNCQ ENEAVHAYLN EVVTLGSPIK QVNYFDVKQS
MQNGGGPACL RLRVAMNDME LAAVNQHTLM NDALFTRLNA WVDKHYRDRL SVDDLADPQV
LIESRTALDE LTQIMKLGSV YQFQK
