ASTB_SHEPA
ID ASTB_SHEPA Reviewed; 445 AA.
AC A8H2S2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=Spea_1534;
OS Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=398579;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700345 / ANG-SQ1;
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.Z., Manno D., Hawari J., Richardson P.;
RT "Complete sequence of Shewanella pealeana ATCC 700345.";
RL Submitted (OCT-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; CP000851; ABV86859.1; -; Genomic_DNA.
DR RefSeq; WP_012154783.1; NC_009901.1.
DR AlphaFoldDB; A8H2S2; -.
DR SMR; A8H2S2; -.
DR STRING; 398579.Spea_1534; -.
DR EnsemblBacteria; ABV86859; ABV86859; Spea_1534.
DR KEGG; spl:Spea_1534; -.
DR eggNOG; COG3724; Bacteria.
DR HOGENOM; CLU_053835_0_0_6; -.
DR OMA; IAPTNCQ; -.
DR UniPathway; UPA00185; UER00280.
DR Proteomes; UP000002608; 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; Reference proteome.
FT CHAIN 1..445
FT /note="N-succinylarginine dihydrolase"
FT /id="PRO_1000085399"
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; 48871 MW; B2DFB3F3331E0CEE CRC64;
MKHFEANFDG LVGPTHNYAG LSFGNVASLN NAAATSSPKD AAKQGLKKAK ALADLGLVQG
MLAPQERPDL HTLRRIGFSG TDAEILNKAA KEAPALLRAC CSASSMWTAN AATVSPSADT
HDGKLHFTPA NLVDKLHRSI EPTTTGNILQ ATFNDSRYFK HHQHLPEHTS FGDEGAANHT
RLCSEYGHAG VELFVYGQEA TNPSAPKPQK FPARQTLEAS QAVARLHQLD DNGTVYIQQN
PDVIDQGVFH NDVIAVGNQN VLFYHEQAFL NTQAKLTEIK NKFGDSALHF VEVPTSQVAI
QDAVKSYLFN TQVVTLPSGE MAIIAPTNCQ ENPAVFAYLN ELVTLDTPIK QVLYFDVKQS
MQNGGGPACL RLRVAMNQDE VAAVNQHTLM NDALFTRLNQ WVDKHYRDRL LVEDLADPQL
VIESRTALDE LTQIMKLGSV YQFQR