ASTB_BURVG
ID ASTB_BURVG Reviewed; 446 AA.
AC A4JCW1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Bcep1808_1103;
OS Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS (strain R1808)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=269482;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G4 / LMG 22486;
RG US DOE Joint Genome Institute;
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., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000614; ABO54114.1; -; Genomic_DNA.
DR AlphaFoldDB; A4JCW1; -.
DR SMR; A4JCW1; -.
DR STRING; 269482.Bcep1808_1103; -.
DR EnsemblBacteria; ABO54114; ABO54114; Bcep1808_1103.
DR KEGG; bvi:Bcep1808_1103; -.
DR eggNOG; COG3724; Bacteria.
DR HOGENOM; CLU_053835_0_0_4; -.
DR OMA; TLNDWVD; -.
DR UniPathway; UPA00185; UER00280.
DR Proteomes; UP000002287; Chromosome 1.
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; Reference proteome.
FT CHAIN 1..446
FT /note="N-succinylarginine dihydrolase"
FT /id="PRO_1000065721"
FT ACT_SITE 174
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT ACT_SITE 249
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT ACT_SITE 370
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 213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
SQ SEQUENCE 446 AA; 48133 MW; C1C9F7D39E6A5E04 CRC64;
MNAQEANFDG LVGPTHNYAG LSFGNVASLN NEKSAANPKA AAKQGLRKMK QLADLGFAQG
VLPPQERPSL RLLRELGFSG KDADVIAKAA KQAPELLAAA SSASAMWTAN AATVSPSADT
ADGRVHFTPA NLCSKLHRAI EHEATRRTLS TLFADPARFV VHDALTGTPA LGDEGAANHT
RFCAAYGKPG VEFFVYGRAE YRRGPEPKRF PARQTFEASR AVAQRHGLDE TATVYAQQDP
DVIDAGVFHN DVISVGNRDT LFTHERAFVN KQAVYDTLTA ALDARGARLN VIEVPDAAVS
VNDAVTSYLF NSQLLSRADG SQVLVVPQEC RENANVAAYL DRLAAANGPI GDVLVFDLRE
SMKNGGGPAC LRLRVVLTDA ERAAVTSNVW MNDTLFASLD AWIDTHYRDR IAPEDLADPA
LLDESRTALD ELTQILRVGS LYDFQR
