ARLY_BRUAB
ID ARLY_BRUAB Reviewed; 466 AA.
AC Q57AS3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Argininosuccinate lyase {ECO:0000255|HAMAP-Rule:MF_00006};
DE Short=ASAL {ECO:0000255|HAMAP-Rule:MF_00006};
DE EC=4.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00006};
DE AltName: Full=Arginosuccinase {ECO:0000255|HAMAP-Rule:MF_00006};
GN Name=argH {ECO:0000255|HAMAP-Rule:MF_00006}; OrderedLocusNames=BruAb1_1957;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(N(omega)-L-arginino)succinate = fumarate + L-arginine;
CC Xref=Rhea:RHEA:24020, ChEBI:CHEBI:29806, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:57472; EC=4.3.2.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00006};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 3/3. {ECO:0000255|HAMAP-
CC Rule:MF_00006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00006}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00006}.
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DR EMBL; AE017223; AAX75261.1; -; Genomic_DNA.
DR RefSeq; WP_002965047.1; NC_006932.1.
DR AlphaFoldDB; Q57AS3; -.
DR SMR; Q57AS3; -.
DR EnsemblBacteria; AAX75261; AAX75261; BruAb1_1957.
DR GeneID; 3788443; -.
DR KEGG; bmb:BruAb1_1957; -.
DR HOGENOM; CLU_027272_2_3_5; -.
DR OMA; KKNPDVF; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000000540; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
DR CDD; cd01359; Argininosuccinate_lyase; 1.
DR Gene3D; 1.10.275.10; -; 1.
DR HAMAP; MF_00006; Arg_succ_lyase; 1.
DR InterPro; IPR029419; Arg_succ_lyase_C.
DR InterPro; IPR009049; Argininosuccinate_lyase.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR PANTHER; PTHR43814; PTHR43814; 1.
DR Pfam; PF14698; ASL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR00838; argH; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Lyase.
FT CHAIN 1..466
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000240716"
SQ SEQUENCE 466 AA; 51267 MW; A455713E39E31C66 CRC64;
MSEQKSSNQM WGGRFASGPD AIMEEINASI GFDRKLYAQD IQGSLAHAAM LAKTGIIAAE
DHKQIENGLK TIRKEIEEGK FTFSRKLEDI HMNIEARLAE LIGPAAGRLH TARSRNDQVA
VDFRLWVKQE LEKTAAALKN LIEAFLERAE EHAATVMPGF THLQTAQPVT FGHHCMAYVE
MFGRDLSRVR DAIERIDESP LGAAALAGTG FPIDRHMTAK ALGFREPTRN SLDSVSDRDY
ALEFLSLAAI CAGHLSRLAE EIVIWSTPQF NFVRLSDAFS TGSSIMPQKK NPDAAELVRA
KTGRINGSLV ALLTIMKGLP LAYSKDMQED KEQVFDAAEN LELAIAAMAG MVRDLTVNVA
AMKKAAGSGY STATDLADWL VRTLGLPFRE AHHVTGRAVA LAESRKVDLA KLSLEELQSI
NPAITAEVFG YLTVEKSVKS RQSFGGTAPQ EVRRQIRYWK KRIAKA
