ID   ARLY_STRCL              Reviewed;         473 AA.
AC   P50988;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2002, sequence version 2.
DT   25-MAY-2022, entry version 104.
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};
OS   Streptomyces clavuligerus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC   3585 / VKM Ac-602;
RX   PubMed=11075930;
RA   Rodriguez-Garcia A., de la Fuente A., Perez-Redondo R., Martin J.F.,
RA   Liras P.;
RT   "Characterization and expression of the arginine biosynthesis gene cluster
RT   of Streptomyces clavuligerus.";
RL   J. Mol. Microbiol. Biotechnol. 2:543-550(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-110.
RC   STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC   3585 / VKM Ac-602;
RX   PubMed=8566818; DOI=10.1016/0378-1119(95)00667-2;
RA   Rodriguez-Garcia A., Martin J.F., Liras P.;
RT   "The argG gene of Streptomyces clavuligerus has low homology to unstable
RT   argG from other actinomycetes: effect of amplification on clavulanic acid
RT   biosynthesis.";
RL   Gene 167:9-15(1995).
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; Z49111; CAA88927.2; -; Genomic_DNA.
DR   PIR; PC4128; S57660.
DR   AlphaFoldDB; P50988; -.
DR   SMR; P50988; -.
DR   STRING; 443255.SCLAV_0795; -.
DR   eggNOG; COG0165; Bacteria.
DR   UniPathway; UPA00068; UER00114.
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..473
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_0000137832"
SQ   SEQUENCE   473 AA;  50941 MW;  44D15442BCC28E94 CRC64;
     MSSNNGDVRL WGGRFADGPA DALARLSASV HFDWRLAPYD IAGSRAHARV LNRAGLLTED
     ELTRMLAGLD RWPPMWRTLL HRTIADEDVH TALERGLLER LGAELGGKLR AGRSRNDQVA
     TLFRMYLRTT PGSSGLIAEL QDALVGLAEA HPEVAMPGRT HLQHAQPVLF AHHVLAHVQA
     LSRDAERLRQ WDARTAVSPY GSGALAGSSL GLDPEAVAAD LGFEGGSAGN SIDGTASRDF
     VAEFAFITAM AGINLSRLAE EIIIWNTKEF SFVTLHDAFS TGSSIMPQKK NPDIAELARG
     KSGRLIGNLT GLLATLKALP LAYNRDLQED KEPVFDSCDQ LEVLLPAFTG MVATLTVHRE
     RMEELAPAGF SLATDIAEWL VRQGVPFRVA HDVAGACVKE CESAGIELHQ LTDEQFAAIS
     EHLTPEVRSV LTVRGALASR DGRGGTAPSA VAVQLAEVKA DLAVQHAWAA RES