ID ASTB_AERHH Reviewed; 445 AA. AC A0KMV4; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 16-JUN-2009, entry version 15. DE RecName: Full=N-succinylarginine dihydrolase; DE EC=3.5.3.23; GN Name=astB; OrderedLocusNames=AHA_3105; OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=380703; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16980456; DOI=10.1128/JB.00621-06; RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., RA Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., RA Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.; RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all RT trades."; RL J. Bacteriol. 188:8272-8282(2006). CC -!- FUNCTION: Catalyzes the hydrolysis of N(2)-succinylarginine into CC N(2)-succinylornithine, ammonia and CO(2) (By similarity). CC -!- CATALYTIC ACTIVITY: N(2)-succinyl-L-arginine + 2 H(2)O = N(2)- CC succinyl-L-ornithine + 2 NH(3) + CO(2). CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST CC pathway; L-glutamate and succinate from L-arginine: step 2/5. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the succinylarginine dihydrolase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000462; ABK38175.1; -; Genomic_DNA. DR RefSeq; YP_857605.1; -. DR GeneID; 4489032; -. DR GenomeReviews; CP000462_GR; AHA_3105. DR KEGG; aha:AHA_3105; -. DR TIGR; AHA_3105; -. DR OMA; A0KMV4; HFAHHPA. DR GO; GO:0009015; F:N-succinylarginine dihydrolase activity; IEA:HAMAP. DR GO; GO:0019544; P:arginine catabolic process to glutamate; IEA:HAMAP. DR HAMAP; MF_01172; -; 1. DR InterPro; IPR007079; SuccinylArg_d-Hdrlase_AstB. DR Gene3D; G3DSA:3.75.10.20; SuccinylArg_di_hydro; 1. DR Pfam; PF04996; AstB; 1. DR TIGRFAMs; TIGR03241; arg_catab_astB; 1. PE 3: Inferred from homology; KW Arginine metabolism; Complete proteome; Hydrolase. FT CHAIN 1 445 N-succinylarginine dihydrolase. FT /FTId=PRO_1000065713. FT REGION 19 28 Substrate binding (By similarity). FT REGION 137 138 Substrate binding (By similarity). FT ACT_SITE 174 174 By similarity. FT ACT_SITE 250 250 By similarity. FT ACT_SITE 369 369 Nucleophile (By similarity). FT BINDING 110 110 Substrate (By similarity). FT BINDING 214 214 Substrate (By similarity). FT BINDING 252 252 Substrate (By similarity). FT BINDING 363 363 Substrate (By similarity). SQ SEQUENCE 445 AA; 48686 MW; 52E4B9CBFC418B75 CRC64; MKHFEVNFDG LVGPTHNYAG LSYGNVASQN NAKEASNPKE AAKQGLRKMK ALTELGMTQG VLAPQERPDL ATLRRLGFTG NDASVLAQAA KQAPAVLAAC YSASSMWTAN AATVSPSADT QDGRIHFTPA NLTNKFHRSL EPEVTGRILR AVFNNDRHFY HHQHLPENDH FGDEGAANHT RLCRAYGESG VELFVYGRSA FDVSQPAPKR YPARQTLEAS QAIARLHGLG DESAVFIQQN PDVIDQGVFH NDVIAVGNQN VLFFHQQAFL NTASALAEVR TKFGDGELHF IEVPTAEVSV QDAVKSYLFN TQILTLPSGE MAIIAPTECR DNPAVSAYLT KLVTLGTPIK GVHYMDVKQS MRNGGGPACL RLRVAMNDTE LAAVNPACLI TDSQFARLDG WVDRHYRDSL ALDDLRDPAL VMESRTALDE LTQILKLGSV YPFQR //