ASTB_SALTI
ID ASTB_SALTI Reviewed; 447 AA.
AC Q8Z6G2; Q7CA94;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=N-succinylarginine dihydrolase {ECO:0000255|HAMAP-Rule:MF_01172};
DE EC=3.5.3.23 {ECO:0000255|HAMAP-Rule:MF_01172};
GN Name=astB {ECO:0000255|HAMAP-Rule:MF_01172};
GN OrderedLocusNames=STY1808, t1185;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- FUNCTION: Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-
CC succinylornithine, ammonia and CO(2). {ECO:0000255|HAMAP-
CC Rule:MF_01172}.
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:0000255|HAMAP-Rule:MF_01172};
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC pathway; L-glutamate and succinate from L-arginine: step 2/5.
CC {ECO:0000255|HAMAP-Rule:MF_01172}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01172}.
CC -!- SIMILARITY: Belongs to the succinylarginine dihydrolase family.
CC {ECO:0000255|HAMAP-Rule:MF_01172}.
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DR EMBL; AL513382; CAD02048.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO68841.1; -; Genomic_DNA.
DR RefSeq; NP_456206.1; NC_003198.1.
DR RefSeq; WP_000123947.1; NZ_WSUR01000034.1.
DR AlphaFoldDB; Q8Z6G2; -.
DR SMR; Q8Z6G2; -.
DR STRING; 220341.16502885; -.
DR EnsemblBacteria; AAO68841; AAO68841; t1185.
DR KEGG; stt:t1185; -.
DR KEGG; sty:STY1808; -.
DR PATRIC; fig|220341.7.peg.1820; -.
DR eggNOG; COG3724; Bacteria.
DR HOGENOM; CLU_053835_0_0_6; -.
DR OMA; TLNDWVD; -.
DR UniPathway; UPA00185; UER00280.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0009015; F:N-succinylarginine dihydrolase activity; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Arginine metabolism; Hydrolase.
FT CHAIN 1..447
FT /note="N-succinylarginine dihydrolase"
FT /id="PRO_0000262372"
FT ACT_SITE 174
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT ACT_SITE 248
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT ACT_SITE 365
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 19..28
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 137..138
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
SQ SEQUENCE 447 AA; 49139 MW; 6E7D8A6491ADE4FA CRC64;
MTAHEVNFDG LVGLTHHYAG LSFGNEASTR HRFQVSNPRL AVKQGLLKMK ALADAGFPQA
VIPPHERPFI PALRQLGFTG SDEQILDKVA RQAPRWLSSV SSASPMWVAN AATVCPSADA
LDGKVHLTVA NLNNKFHRAL EAPVTEALLR AIFRDESQFS VHSALPQVAL LGDEGAANHN
RLGGEYGSAG VQLFVYGREE ENEIRPARYP ARQSREASEA VARLNQVNPQ QVIFAQQNPE
VIDQGVFHND VIAVSNRQVL FCHEAAFARQ KVLINQLRTR VDGFMAIEVP AGEVSVSDAV
ATYLFNSQLL SRDDGSMLLV LPRECQDHAG VWRYLNKLVA EDNPISAMQV FDLRESMANG
GGPACLRLRV VLTEEERRAV NPAVMMNDAL FTALNAWADR YYRDRLTAAD LADPLLLREG
REALDVLTRL LDLGSVYPFQ QTGAADG
