ID   ARLY_CLOK1              Reviewed;         438 AA.
AC   B9E0B2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 62.
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=CKR_0886;
OS   Clostridium kluyveri (strain NBRC 12016).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=583346;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 12016;
RA   Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., Vertes A.A.,
RA   Yukawa H.;
RT   "Complete genome sequence of Clostridium kluyveri and comparative genomics
RT   of Clostridia species.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; AP009049; BAH05937.1; -; Genomic_DNA.
DR   RefSeq; WP_012101354.1; NC_011837.1.
DR   AlphaFoldDB; B9E0B2; -.
DR   SMR; B9E0B2; -.
DR   EnsemblBacteria; BAH05937; BAH05937; CKR_0886.
DR   KEGG; ckr:CKR_0886; -.
DR   HOGENOM; CLU_027272_2_3_9; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000007969; Chromosome.
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..438
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000116317"
SQ   SEQUENCE   438 AA;  50221 MW;  B9A7988133457D25 CRC64;
     MKLWGGRFKK SESKLMEDFN SSLSFDRQLY KEDIEGSMVH VKMLAKCNIL SSEESKAILS
     GLESILKDIE EGKLEVEGDY EDIHSFVEIN LIERIGQVAK KLHTARSRND QVALDFRLYA
     KRKALEVVEN IEYLQDVIEN LGDKNNVIMP GYTHLQRAQV VTFKHHIMAY YHMFKRDRER
     ILNAICIMDE SPLGCCALAG TTYNIDRNFT AQELGFKKPV DNFLDGVSDR DYVIELISDF
     SIIMMHLSRL SEELILWSSK EFDFIRIDDE FSTGSSIMPQ KKNPDAAELI RGKTGRVYGS
     LVSLLTTMKG IPLAYNKDMQ EDKEQLFNSL DTVLSCLKIM SGMLSTLKVN EKNTFNAVKK
     GFLNATEAAD YLVNKGMAFR DAHKVIGEIV LYCEDKNRAI EDISLDELKK FSSLFEEDVY
     DFIDYENTIN RGIKRNLK