ASTB_SHEB8
ID ASTB_SHEB8 Reviewed; 444 AA.
AC A6WP88;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
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};
GN OrderedLocusNames=Shew185_2490;
OS Shewanella baltica (strain OS185).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=402882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS185;
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., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brettar I., Rodrigues J., Konstantinidis K., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS185.";
RL Submitted (JUL-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; CP000753; ABS08627.1; -; Genomic_DNA.
DR RefSeq; WP_006086245.1; NC_009665.1.
DR AlphaFoldDB; A6WP88; -.
DR SMR; A6WP88; -.
DR GeneID; 11772705; -.
DR KEGG; sbm:Shew185_2490; -.
DR HOGENOM; CLU_053835_0_0_6; -.
DR OMA; IAPTNCQ; -.
DR UniPathway; UPA00185; UER00280.
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..444
FT /note="N-succinylarginine dihydrolase"
FT /id="PRO_1000065737"
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 368
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 362
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
SQ SEQUENCE 444 AA; 49176 MW; 9F0A1E5B99A9C6A4 CRC64;
MKHFEANFDG LVGPTHNYAG LSFGNVASLS NAALVSNPKA AAKQGLQKAK ALADMGMVQG
MLAPQERPDL YTLRRIGFSG SDANVLKQAA KEAPMLLNAC CSASSMWTAN AATVSPSADT
RDGKLHFTPA NLVDKLHRSI EPLTTGRILT ATFSDPHYFH HHSHLPEHNS FGDEGAANQT
RLCNEYGHAG VELFVYGQEA TNPNAPKPQK YPARQTLEAS MAVARLHQLE EDNCVFIQQN
PDVIDQGVFH NDVIAVGNQN VLFYHEQAFL NTQHKIDEIK RKLDTELYFI EVPTAKVAIN
DAVKSYLFNT QIITLPSGEM AIIAPTDCQE NPAVFAYLNE LLTLNTPIKQ VLYFDVKQSM
QNGGGPACLR LRVAMNEMEV AAVNQHTLMN DALFARLNLW VDKHYRDRLT TQDLADPQLI
IESRTALDEL TQIMKLGSVY QFQR
