ID   ASTB_SHESA              Reviewed;         444 AA.
AC   A0KVZ2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   16-JUN-2009, entry version 16.
DE   RecName: Full=N-succinylarginine dihydrolase;
DE            EC=3.5.3.23;
GN   Name=astB; OrderedLocusNames=Shewana3_1728;
OS   Shewanella sp. (strain ANA-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=94122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Newman D., Salticov C., Konstantinidis K., Klappenback J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000469; ABK47961.1; -; Genomic_DNA.
DR   RefSeq; YP_869367.1; -.
DR   GeneID; 4479561; -.
DR   GenomeReviews; CP000469_GR; Shewana3_1728.
DR   KEGG; shn:Shewana3_1728; -.
DR   NMPDR; fig|94122.5.peg.1807; -.
DR   OMA; A0KVZ2; 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    444       N-succinylarginine dihydrolase.
FT                                /FTId=PRO_1000065740.
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;  49067 MW;  177FE5A4F50AA203 CRC64;
     MKHFEANFDG LVGPTHNYAG LSFGNVASLN NAALVSNPKA AAKQGLQKAK ALADLGMIQG
     MLAPQERPDL NTLRRIGFSG SDAQVLQQAA KTAPALLNAC CSASSMWTAN AATVSPSADT
     RDGKLHFTPA NLVDKLHRSI EPTTTGRILT ATFNDPHYFH HHNHLPEHNS FGDEGAANHT
     RLCQEYGHAG VELFVYGQEA TNPNAPRPQK YPARQTLEAS MAIARLHQLE EDNCVFIQQN
     PDVIDQGVFH NDVIAVGNQN VLFYHEQAFL NTQAKLDEIR RKLDTELFFI EVPTTKVAIN
     NAVKSYLFNT QIITLPSGEM AIIAPTDCQE NPAVYAYLNE LLTLNTPIKQ VLYFDVKQSM
     QNGGGPACLR LRVAMNEREV AAANQHTLLN DALFARLNTW VDKHYRDRLS TQDLADPQLV
     VESRTALDEL TQIMKLGSVY PFQR
//