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 03-AUG-2022, entry version 154.
DE RecName: Full=N-succinylarginine dihydrolase;
DE EC=3.5.3.23 {ECO:0000269|PubMed:15703173};
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; DOI=10.1128/jb.180.16.4278-4286.1998;
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, CATALYTIC ACTIVITY, SUBUNIT,
RP AND MUTAGENESIS OF 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 Evidence={ECO:0000269|PubMed:15703173};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19534;
CC Evidence={ECO:0000305|PubMed:15703173};
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC pathway; L-glutamate and succinate from L-arginine: step 2/5.
CC {ECO:0000305|PubMed:15703173}.
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}.
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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 AlphaFoldDB; P76216; -.
DR SMR; P76216; -.
DR BioGRID; 4262234; 10.
DR IntAct; P76216; 1.
DR STRING; 511145.b1745; -.
DR DrugBank; DB02501; N(2)-succinyl-L-arginine.
DR DrugBank; DB03582; N~2~-Succinylornithine.
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; COG3724; Bacteria.
DR HOGENOM; CLU_053835_0_0_6; -.
DR InParanoid; P76216; -.
DR OMA; TLNDWVD; -.
DR PhylomeDB; P76216; -.
DR BioCyc; EcoCyc:SUCCARGDIHYDRO-MON; -.
DR BioCyc; MetaCyc:SUCCARGDIHYDRO-MON; -.
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 DisProt; DP02760; -.
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;
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 ACT_SITE 174
FT ACT_SITE 248
FT ACT_SITE 365
FT /note="Nucleophile"
FT BINDING 19..28
FT /ligand="substrate"
FT BINDING 110
FT /ligand="substrate"
FT BINDING 137..138
FT /ligand="substrate"
FT BINDING 212
FT /ligand="substrate"
FT BINDING 250
FT /ligand="substrate"
FT BINDING 359
FT /ligand="substrate"
FT MUTAGEN 365
FT /note="C->S: Large decrease in N-succinylarginine
FT dihydrolase activity."
FT /evidence="ECO:0000269|PubMed:15703173"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 26..30
FT /evidence="ECO:0007829|PDB:1YNH"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:1YNH"
FT HELIX 38..54
FT /evidence="ECO:0007829|PDB:1YNF"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 70..75
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 82..92
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 95..99
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1YNF"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:1YNF"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:1YNF"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 142..152
FT /evidence="ECO:0007829|PDB:1YNF"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:1YNF"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:1YNF"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:1YNF"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:1YNF"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:1YNF"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:1YNF"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:1YNF"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:1YNF"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 270..280
FT /evidence="ECO:0007829|PDB:1YNF"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:1YNF"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 296..302
FT /evidence="ECO:0007829|PDB:1YNF"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:1YNF"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:1YNF"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 329..340
FT /evidence="ECO:0007829|PDB:1YNF"
FT STRAND 341..351
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:1YNF"
FT TURN 363..366
FT /evidence="ECO:0007829|PDB:1YNF"
FT STRAND 367..372
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 374..379
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 388..401
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 408..412
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 414..430
FT /evidence="ECO:0007829|PDB:1YNF"
FT HELIX 438..440
FT /evidence="ECO:0007829|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
