ID   ARLY_STRCO              Reviewed;         475 AA.
AC   Q9L1B1;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 120.
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=SCO1570;
GN   ORFNames=SCL24.06c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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; AL939109; CAB76090.1; -; Genomic_DNA.
DR   RefSeq; NP_625847.1; NC_003888.3.
DR   RefSeq; WP_011027854.1; NZ_VNID01000021.1.
DR   AlphaFoldDB; Q9L1B1; -.
DR   SMR; Q9L1B1; -.
DR   STRING; 100226.SCO1570; -.
DR   GeneID; 1097001; -.
DR   KEGG; sco:SCO1570; -.
DR   PATRIC; fig|100226.15.peg.1582; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_2_11; -.
DR   InParanoid; Q9L1B1; -.
DR   OMA; KKNPDVF; -.
DR   PhylomeDB; Q9L1B1; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IBA:GO_Central.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
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..475
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_0000137833"
SQ   SEQUENCE   475 AA;  50942 MW;  9E2EB1448589A509 CRC64;
     MSSNSGDVRL WGGRFADGPA EALAKLSASV HFDWRLAPYD IAGSRAHARV LHAAGLLTED
     ELTRMIAGLD RLEADVADGS FTGTIADEDV HTALERGLLE RLGPDLGGKL RAGRSRNDQV
     ATLFRMYLRD HARTVGSLIA DLQDALVGLA EAHPDVAMPG RTHLQHAQPV LFAHHVLAHA
     QALGRDAERL RQWDARTAVS PYGSGALAGS SLGLDPEAVA RDLGFEHGSV GNSIDGTASR
     DFVAEFAFIT AMIGVNVSRI AEEIIIWNTK EFSFVTLHDA FSTGSSIMPQ KKNPDIAELA
     RGKSGRLIGN LTGLMATLKA LPLAYNRDLQ EDKEPVFDSI DQLEVLLPAF TGMMATLTVH
     RERMEELAPA GFSLATDIAE WLVKQGVPFR VAHEVAGECV KVAEADGKEL DELTDEQFAK
     ISEHLTPEVR TVLNVPGALA SRDGRGGTAP SAVAVQLAEV KADVAAQHAW ADAKK