ARLY_CLOBJ
ID ARLY_CLOBJ Reviewed; 440 AA.
AC C1FU67;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 65.
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=CLM_3034;
OS Clostridium botulinum (strain Kyoto / Type A2).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kyoto / Type A2;
RA Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL Submitted (OCT-2008) 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; CP001581; ACO83787.1; -; Genomic_DNA.
DR RefSeq; WP_012703877.1; NC_012563.1.
DR AlphaFoldDB; C1FU67; -.
DR SMR; C1FU67; -.
DR STRING; 536232.CLM_3034; -.
DR PRIDE; C1FU67; -.
DR EnsemblBacteria; ACO83787; ACO83787; CLM_3034.
DR KEGG; cby:CLM_3034; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_9; -.
DR OMA; KKNPDVF; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000001374; 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..440
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000116315"
SQ SEQUENCE 440 AA; 50510 MW; 8D72BC987E2E165D CRC64;
MKLWGGRFKE EESKLMEDFN SSLSFDKKLY YEDIKGSIAH VKMLTNQNII KEEEKEKILL
GLEEILKEID EGILKIEGDY EDIHSFVEIN LINKIGNVGK KLHTGRSRND QVALDMKLYA
KKSTEEVIEC LKELMDSLIK VGNENNYIMP GYTHLQRAQV VTFRYHLLAY FEMFKRDEKR
LENALEILNE SPLGSGALAG STYNIDREYT AKLLGFRKPV DNFLDGVSDR DYIIELISKF
SIIMMHLSRL SEELILWSSS EFRFIQIGDA YSTGSSIMPQ KKNPDGAELI RGKIGRVYGD
LISILTVMKS LPLAYNKDMQ EDKEPFFDAK DTVISCLKVM EGIISTLKVN KENLMKSVKK
GFLNATEAAD YLVNKGMAFR DAHKVIGEVV IYCEDKNSAI EDLSLEELKQ FSDLFCEDIY
EFIDYKNSIN KGIKKEMGYF
