ASTA_YERPE
ID ASTA_YERPE Reviewed; 350 AA.
AC Q9ZC67; Q74UK5; Q7CI71;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Arginine N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_01171};
DE Short=AST {ECO:0000255|HAMAP-Rule:MF_01171};
DE EC=2.3.1.109 {ECO:0000255|HAMAP-Rule:MF_01171};
DE AltName: Full=AOST {ECO:0000255|HAMAP-Rule:MF_01171};
GN Name=astA {ECO:0000255|HAMAP-Rule:MF_01171};
GN OrderedLocusNames=YPO1963, y2348, YP_1708;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=6/69;
RA Buchrieser C., Rusniok C., Couve E., Frangeul L., Billault A., Kunst F.,
RA Carniel E., Glaser P.;
RT "DNA sequence of the 102 kbases unstable region of Yersinia pestis.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
CC -!- FUNCTION: Catalyzes the transfer of succinyl-CoA to arginine to produce
CC N(2)-succinylarginine. {ECO:0000255|HAMAP-Rule:MF_01171}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginine + succinyl-CoA = CoA + H(+) + N(2)-succinyl-L-
CC arginine; Xref=Rhea:RHEA:15185, ChEBI:CHEBI:15378, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:58241;
CC EC=2.3.1.109; Evidence={ECO:0000255|HAMAP-Rule:MF_01171};
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC pathway; L-glutamate and succinate from L-arginine: step 1/5.
CC {ECO:0000255|HAMAP-Rule:MF_01171}.
CC -!- SIMILARITY: Belongs to the arginine N-succinyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_01171}.
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DR EMBL; AL031866; CAA21340.1; -; Genomic_DNA.
DR EMBL; AL590842; CAL20601.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS61937.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM85906.1; -; Genomic_DNA.
DR PIR; AF0239; AF0239.
DR PIR; T46997; T46997.
DR RefSeq; WP_002212031.1; NZ_UHIZ01000001.1.
DR RefSeq; YP_002346952.1; NC_003143.1.
DR AlphaFoldDB; Q9ZC67; -.
DR SMR; Q9ZC67; -.
DR STRING; 214092.YPO1963; -.
DR PaxDb; Q9ZC67; -.
DR DNASU; 1147295; -.
DR EnsemblBacteria; AAM85906; AAM85906; y2348.
DR EnsemblBacteria; AAS61937; AAS61937; YP_1708.
DR KEGG; ype:YPO1963; -.
DR KEGG; ypk:y2348; -.
DR KEGG; ypm:YP_1708; -.
DR PATRIC; fig|214092.21.peg.2340; -.
DR eggNOG; COG3138; Bacteria.
DR HOGENOM; CLU_057655_0_0_6; -.
DR OMA; PEENRSW; -.
DR UniPathway; UPA00185; UER00279.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0008791; F:arginine N-succinyltransferase 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 HAMAP; MF_01171; AstA; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR007041; Arg_succinylTrfase_AstA/AruG.
DR InterPro; IPR017650; Arginine_N-succinylTrfase.
DR Pfam; PF04958; AstA; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR TIGRFAMs; TIGR03243; arg_catab_AOST; 1.
DR TIGRFAMs; TIGR03244; arg_catab_AstA; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Arginine metabolism; Reference proteome; Transferase.
FT CHAIN 1..350
FT /note="Arginine N-succinyltransferase"
FT /id="PRO_0000262335"
FT ACT_SITE 229
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01171"
FT BINDING 125
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01171"
SQ SEQUENCE 350 AA; 39468 MW; 1F3C02A1B04C92BD CRC64;
MMKVRPVERR DLADIFELAG KTGVGMTSLP QNEQHLAARI ERALNTWQGS LDPGEQGYLF
VLEDSEQQKV VGVSAIEVAV GLNDPWYNFR VGTLVHASKA LNVYKSVPTL FLSNDHTGYS
ELCTLFLDPD YRKDKNGPFL SKVRFLFIAA FRQYFSRKVI AEMRGYTDEQ GRSPFWESVG
RHFFSIEFAK ADYLSGTGQK AFIAELMPKH PLYVDFLAEE ARAVIGQVHP HTAPARAVLE
TEGLQYQGYV DIFDGGPTLE ANTDDVRVVR DSSKRTVVIK DYDIEDYDID PNGRLYLVAN
DHYHHFRAIL MNTHLSDERL RLTPESAEAL GVAAGDSVRI VSLFAPETKR
