ID   ASTB_SHEON              Reviewed;         444 AA.
AC   Q8EDN7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 43.
DE   RecName: Full=N-succinylarginine dihydrolase;
DE            EC=3.5.3.23;
GN   Name=astB; OrderedLocusNames=SO_2706;
OS   Shewanella oneidensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=70863;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   MEDLINE=22297686; PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A.,
RA   Clayton R.A., Meyer T., Tsapin A., Scott J., Beanan M.J.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S.,
RA   Haft D.H., Kolonay J.F., Madupu R., Peterson J.D., Umayam L.A.,
RA   White O., Wolf A.M., Vamathevan J.J., Weidman J.F., Impraim M.,
RA   Lee K., Berry K.J., Lee C., Mueller J., Khouri H.M., Gill J.,
RA   Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O.,
RA   Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
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.
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DR   EMBL; AE014299; AAN55734.1; -; Genomic_DNA.
DR   RefSeq; NP_718290.1; -.
DR   GeneID; 1170407; -.
DR   GenomeReviews; AE014299_GR; SO_2706.
DR   KEGG; son:SO_2706; -.
DR   NMPDR; fig|211586.1.peg.2459; -.
DR   TIGR; SO_2706; -.
DR   HOGENOM; Q8EDN7; -.
DR   OMA; Q8EDN7; KMKALME.
DR   BioCyc; SONE211586:SO_2706-MON; -.
DR   BRENDA; 3.5.3.23; 257422.
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    444       N-succinylarginine dihydrolase.
FT                                /FTId=PRO_0000262376.
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    368    368       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     362    362       Substrate (By similarity).
SQ   SEQUENCE   444 AA;  49061 MW;  BD0619B1A831ECCF CRC64;
     MKHFEANFDG LVGPTHNYAG LSFGNVASLN NAALVSNPKA AAKQGLQKAK ALADLGMIQG
     MLAPQERPDL NTLRRIGFSG SDAQVLQQAA KTAPALLNAC CSASSMWTAN AATVSPSADT
     RDGKLHFTPA NLVDKLHRSI EPITTGRILT ATFNDPHYFY HHNHLPEHNS FGDEGAANHT
     RLCQEYGHAG VELFVYGQEA TNPHAPKPLK FPARQTLEAS MAIARLHQLE EDNCVFIQQN
     PAVIDQGVFH NDVIAVGNQN VLFYHEQAFL NTQAKLDEIK RKLDTELYFI EVPTAKVSIN
     DAVKSYLFNT QIITLPSGEM AIIAPTDCQE NPAVYAYLNE LLSLNTPIKQ VLYFDVKQSM
     QNGGGPACLR LRVAMNEREV AAVNQHTLLT DALFTRLNTW VEKHYRDRLS TEDLADPQLV
     IESRTALDEL TQIMKLGSVY PFQR
//