ASTB_ZYMMO
ID ASTB_ZYMMO Reviewed; 424 AA.
AC Q5NNB4; Q9X3V5; Q9X5D4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
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}; OrderedLocusNames=ZMO1172;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA Lee H.J., Kang H.S.;
RT "Sequence analysis of 42C11 fosmid clone of Zymomonas mobilis ZM4.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA Lee H.J., Kang H.S.;
RT "Sequence analysis of 43D2 fosmid clone of Zymomonas mobilis ZM4.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
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; AF088896; AAD21533.1; -; Genomic_DNA.
DR EMBL; AF124757; AAD29641.1; -; Genomic_DNA.
DR EMBL; AE008692; AAV89796.1; -; Genomic_DNA.
DR RefSeq; WP_011240996.1; NZ_CP035711.1.
DR AlphaFoldDB; Q5NNB4; -.
DR SMR; Q5NNB4; -.
DR STRING; 264203.ZMO1172; -.
DR EnsemblBacteria; AAV89796; AAV89796; ZMO1172.
DR GeneID; 58026945; -.
DR KEGG; zmo:ZMO1172; -.
DR eggNOG; COG3724; Bacteria.
DR HOGENOM; CLU_053835_0_0_5; -.
DR OMA; IAPTNCQ; -.
DR OrthoDB; 567590at2; -.
DR UniPathway; UPA00185; UER00280.
DR Proteomes; UP000001173; 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.
PE 3: Inferred from homology;
KW Arginine metabolism; Hydrolase; Reference proteome.
FT CHAIN 1..424
FT /note="N-succinylarginine dihydrolase"
FT /id="PRO_0000262385"
FT ACT_SITE 174
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT ACT_SITE 242
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT ACT_SITE 357
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 206
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT CONFLICT 91..96
FT /note="KDDRLL -> RMIGCY (in Ref. 1; AAD21533)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="I -> M (in Ref. 1; AAD21533 and 2; AAD29641)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="E -> D (in Ref. 2; AAD29641)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="R -> K (in Ref. 1; AAD21533)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="K -> I (in Ref. 2; AAD29641)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="K -> N (in Ref. 2; AAD29641)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="K -> M (in Ref. 2; AAD29641)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="E -> D (in Ref. 2; AAD29641)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="E -> D (in Ref. 2; AAD29641)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 47270 MW; A26B19E124387C89 CRC64;
MIVSEVNFDG LIGPTHNYAG LSRGNVASAL HAGQPSYPRQ AALQGLEKMK HLMDMGLTQG
VFLPPLRPVT HLLHHLGYKG DDKTILKQAA KDDRLLFNNL CSASSMWAAN AATVISEFDS
HDGRVHFITA NLATMLHRHL EAQTTYAQLN QIFSNSCFFA MHHPLPCGQH FSDEGAANHM
RITSAHGRTG INIFVYGEKN DIYPARQKLR ASQAVARLGE VKPDLAWFIP QKKEAIAKGA
FHNDVVAVAN EYVLLAHAEA FEDQGEWIKR IAEKIDGFIP IIIDNITLEQ AVKSYLFNSQ
IVTLKDRTMA LILPQEVKSD PAVWETVNRI ISGNNPIKKA VVVDVRESMA NGGGPACLRL
RVPLSKAALE AVDQRFILTP KRWEKLYQLV ENFWPEKITP DDLVLPELWK TAVRAHWALT
SWLG
