(data stored in SCRATCH zone)

SWISSPROT: ASTB_ECOLI

ID   ASTB_ECOLI              Reviewed;         447 AA.
AC   P76216; Q2MB40;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   11-DEC-2019, entry version 142.
DE   RecName: Full=N-succinylarginine dihydrolase;
DE            EC=3.5.3.23;
GN   Name=astB; Synonyms=ydjT; OrderedLocusNames=b1745, JW1734;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [3]
RP   FUNCTION.
RX   PubMed=9696779;
RA   Schneider B.L., Kiupakis A.K., Reitzer L.J.;
RT   "Arginine catabolism and the arginine succinyltransferase pathway in
RT   Escherichia coli.";
RL   J. Bacteriol. 180:4278-4286(1998).
RN   [4]
RP   INDUCTION.
RX   PubMed=12003934; DOI=10.1128/jb.184.11.2940-2950.2002;
RA   Kiupakis A.K., Reitzer L.;
RT   "ArgR-independent induction and ArgR-dependent superinduction of the
RT   astCADBE operon in Escherichia coli.";
RL   J. Bacteriol. 184:2940-2950(2002).
RN   [5]
RP   3D-STRUCTURE MODELING.
RX   PubMed=14675764; DOI=10.1016/s0014-5793(03)01314-0;
RA   Shirai H., Mizuguchi K.;
RT   "Prediction of the structure and function of AstA and AstB, the first two
RT   enzymes of the arginine succinyltransferase pathway of arginine
RT   catabolism.";
RL   FEBS Lett. 555:505-510(2003).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-447 OF WILD-TYPE AND MUTANT
RP   SER-365 IN COMPLEXES WITH SUBSTRATE, FUNCTION, SUBUNIT, AND MUTAGENESIS OF
RP   CYS-365.
RX   PubMed=15703173; DOI=10.1074/jbc.m413833200;
RA   Tocilj A., Schrag J.D., Li Y., Schneider B.L., Reitzer L., Matte A.,
RA   Cygler M.;
RT   "Crystal structure of N-succinylarginine dihydrolase AstB, bound to
RT   substrate and product, an enzyme from the arginine catabolic pathway of
RT   Escherichia coli.";
RL   J. Biol. Chem. 280:15800-15808(2005).
CC   -!- FUNCTION: Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-
CC       succinylornithine, ammonia and CO(2). {ECO:0000269|PubMed:15703173,
CC       ECO:0000269|PubMed:9696779}.
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   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC       pathway; L-glutamate and succinate from L-arginine: step 2/5.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15703173}.
CC   -!- INDUCTION: By nitrogen starvation, and arginine. Induced at stationary
CC       phase via sigma S. {ECO:0000269|PubMed:12003934}.
CC   -!- SIMILARITY: Belongs to the succinylarginine dihydrolase family.
CC       {ECO:0000305}.
DR   EMBL; U00096; AAC74815.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76516.1; -; Genomic_DNA.
DR   PIR; A64934; A64934.
DR   RefSeq; NP_416259.1; NC_000913.3.
DR   RefSeq; WP_000994973.1; NZ_SSZK01000001.1.
DR   PDB; 1YNF; X-ray; 1.90 A; A/B/C/D/E/F=2-447.
DR   PDB; 1YNH; X-ray; 1.95 A; A/B/C/D=2-447.
DR   PDB; 1YNI; X-ray; 2.20 A; A/B/C/D=2-447.
DR   PDBsum; 1YNF; -.
DR   PDBsum; 1YNH; -.
DR   PDBsum; 1YNI; -.
DR   SMR; P76216; -.
DR   BioGrid; 4262234; 10.
DR   IntAct; P76216; 1.
DR   STRING; 511145.b1745; -.
DR   DrugBank; DB02501; N~2~-Succinylarginine.
DR   DrugBank; DB03582; N~2~-Succinylornithine.
DR   EPD; P76216; -.
DR   jPOST; P76216; -.
DR   PaxDb; P76216; -.
DR   PRIDE; P76216; -.
DR   EnsemblBacteria; AAC74815; AAC74815; b1745.
DR   EnsemblBacteria; BAE76516; BAE76516; BAE76516.
DR   GeneID; 946259; -.
DR   KEGG; ecj:JW1734; -.
DR   KEGG; eco:b1745; -.
DR   PATRIC; fig|1411691.4.peg.511; -.
DR   EchoBASE; EB3752; -.
DR   eggNOG; ENOG4105EY2; Bacteria.
DR   eggNOG; COG3724; LUCA.
DR   HOGENOM; HOG000226005; -.
DR   InParanoid; P76216; -.
DR   KO; K01484; -.
DR   BioCyc; EcoCyc:SUCCARGDIHYDRO-MONOMER; -.
DR   BioCyc; ECOL316407:JW1734-MONOMER; -.
DR   BioCyc; MetaCyc:SUCCARGDIHYDRO-MONOMER; -.
DR   BRENDA; 3.5.3.23; 2026.
DR   UniPathway; UPA00185; UER00280.
DR   EvolutionaryTrace; P76216; -.
DR   PRO; PR:P76216; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0009015; F:N-succinylarginine dihydrolase activity; IDA:EcoCyc.
DR   GO; GO:0006527; P:arginine catabolic process; IMP:EcoliWiki.
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   1: Evidence at protein level;
DR   PRODOM; P76216.
DR   SWISS-2DPAGE; P76216.
KW   3D-structure; Arginine metabolism; Hydrolase; Reference proteome;
KW   Stress response.
FT   CHAIN           1..447
FT                   /note="N-succinylarginine dihydrolase"
FT                   /id="PRO_0000064715"
FT   REGION          19..28
FT                   /note="Substrate binding"
FT   REGION          137..138
FT                   /note="Substrate binding"
FT   ACT_SITE        174
FT   ACT_SITE        248
FT   ACT_SITE        365
FT                   /note="Nucleophile"
FT   BINDING         110
FT                   /note="Substrate"
FT   BINDING         212
FT                   /note="Substrate"
FT   BINDING         250
FT                   /note="Substrate"
FT   BINDING         359
FT                   /note="Substrate"
FT   MUTAGEN         365
FT                   /note="C->S: Large decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:15703173"
FT   STRAND          4..10
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           26..30
FT                   /evidence="ECO:0000244|PDB:1YNH"
FT   TURN            31..33
FT                   /evidence="ECO:0000244|PDB:1YNH"
FT   HELIX           38..54
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   STRAND          59..62
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           70..75
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           82..92
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           95..99
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           104..106
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           108..110
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   STRAND          112..115
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   TURN            117..119
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   STRAND          123..129
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           136..139
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           142..152
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   TURN            156..158
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   STRAND          159..162
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           169..171
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           175..178
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   STRAND          179..182
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   STRAND          191..198
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   STRAND          207..209
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           215..224
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           229..231
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   STRAND          232..237
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           239..242
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   TURN            243..245
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           249..251
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   STRAND          253..256
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   STRAND          259..263
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           270..280
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   STRAND          285..289
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   TURN            291..293
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           296..302
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   TURN            303..305
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   STRAND          306..311
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   STRAND          317..322
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           323..326
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           329..340
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   STRAND          341..351
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           354..358
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   TURN            363..366
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   STRAND          367..372
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           374..379
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           382..384
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           388..401
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           408..412
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           414..430
FT                   /evidence="ECO:0000244|PDB:1YNF"
FT   HELIX           438..440
FT                   /evidence="ECO:0000244|PDB:1YNF"
SQ   SEQUENCE   447 AA;  49299 MW;  710AE691E413AF64 CRC64;
     MNAWEVNFDG LVGLTHHYAG LSFGNEASTR HRFQVSNPRL AAKQGLLKMK ALADAGFPQA
     VIPPHERPFI PVLRQLGFSG SDEQVLEKVA RQAPHWLSSV SSASPMWVAN AATIAPSADT
     LDGKVHLTVA NLNNKFHRSL EAPVTESLLK AIFNDEEKFS VHSALPQVAL LGDEGAANHN
     RLGGHYGEPG MQLFVYGREE GNDTRPSRYP ARQTREASEA VARLNQVNPQ QVIFAQQNPD
     VIDQGVFHND VIAVSNRQVL FCHQQAFARQ SQLLANLRAR VNGFMAIEVP ATQVSVSDTV
     STYLFNSQLL SRDDGSMMLV LPQECREHAG VWGYLNELLA ADNPISELKV FDLRESMANG
     GGPACLRLRV VLTEEERRAV NPAVMMNDTL FNALNDWVDR YYRDRLTAAD LADPQLLREG
     REALDVLSQL LNLGSVYPFQ REGGGNG
//

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