ID   ARLY_BRUA2              Reviewed;         466 AA.
AC   Q2YR87;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=BAB1_1982;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(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; AM040264; CAJ11938.1; -; Genomic_DNA.
DR   RefSeq; WP_002965047.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YR87; -.
DR   SMR; Q2YR87; -.
DR   STRING; 359391.BAB1_1982; -.
DR   EnsemblBacteria; CAJ11938; CAJ11938; BAB1_1982.
DR   GeneID; 3788443; -.
DR   KEGG; bmf:BAB1_1982; -.
DR   PATRIC; fig|359391.11.peg.1220; -.
DR   HOGENOM; CLU_027272_2_3_5; -.
DR   OMA; KKNPDVF; -.
DR   PhylomeDB; Q2YR87; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000002719; 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;
KW   Reference proteome.
FT   CHAIN           1..466
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_0000240717"
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