ID   ARLY_CLOD6              Reviewed;         438 AA.
AC   Q182I5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 97.
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=CD630_25000;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM180355; CAJ69386.2; -; Genomic_DNA.
DR   RefSeq; WP_009890714.1; NZ_CP010905.2.
DR   RefSeq; YP_001089013.2; NC_009089.1.
DR   AlphaFoldDB; Q182I5; -.
DR   SMR; Q182I5; -.
DR   STRING; 272563.CD630_25000; -.
DR   PRIDE; Q182I5; -.
DR   EnsemblBacteria; CAJ69386; CAJ69386; CD630_25000.
DR   KEGG; cdf:CD630_25000; -.
DR   KEGG; pdc:CDIF630_02747; -.
DR   PATRIC; fig|272563.120.peg.2639; -.
DR   eggNOG; COG0165; Bacteria.
DR   OMA; KKNPDVF; -.
DR   PhylomeDB; Q182I5; -.
DR   BioCyc; PDIF272563:G12WB-2654-MON; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000001978; 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;
KW   Reference proteome.
FT   CHAIN           1..438
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_0000321438"
SQ   SEQUENCE   438 AA;  49853 MW;  74477B6BA81647B4 CRC64;
     MKLWGGRFRK AENQLMEEFN KSFGYDCVLY KKDIEGSVAH VHMQVKCGLL TEEEGKSITE
     GLKGILEDVE NGKLVLDGEY EDIHSFTEIN LIQRIGDVGK KLHTARSRND QVAVDMRLYA
     KEKANDLVGL ISEFKATIKD VADKNPVMMP GYTHLQRAQV VTFKHHLMAY YSMFDRDEKR
     IKNAIEILDE SPLGCGALAG TTHDIDRSIT CEQLGFKKVV DNFMDGVSDR DYLLELMSDF
     SIIMMHLSRL SEELILWSSQ EFGFVEIDDL YTTGSSIMPQ KKNPDGAELI RGKTGRVYGN
     LFGLFTVMKG IPLAYNKDMQ EDKEGFFDSV HTLEMCIQIM DRMIATLKVN EDKMKQAVKN
     GFLNATEVAD YLVKNNVAFR DAHGIVGSIV IYCEDNKKAI EDLTLEELHK FSDAFKEDIY
     DFIDYESILN KGIKKNLK