ARLY_CLOBA
ID ARLY_CLOBA Reviewed; 465 AA.
AC B2UYI1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=CLH_2866;
OS Clostridium botulinum (strain Alaska E43 / Type E3).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=508767;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alaska E43 / Type E3;
RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Complete genome sequence of Clostridium botulinum E3 str. Alaska E43.";
RL Submitted (MAY-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; CP001078; ACD52561.1; -; Genomic_DNA.
DR RefSeq; WP_012450681.1; NC_010723.1.
DR AlphaFoldDB; B2UYI1; -.
DR SMR; B2UYI1; -.
DR PRIDE; B2UYI1; -.
DR KEGG; cbt:CLH_2866; -.
DR HOGENOM; CLU_027272_2_3_9; -.
DR OMA; KKNPDVF; -.
DR OrthoDB; 751464at2; -.
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..465
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000089074"
SQ SEQUENCE 465 AA; 52848 MW; E9509C9D13F51438 CRC64;
MKLWGGRFKK GTDELVNDFN SSINIDSRMY KEDIEGSLAH ASMLGEQNII SKEDSLKITS
GLLEILKRMD NDVINIDLTS EDIHSFVEST LTYYIGEYGK MLHTARSRND QVTLDLKLYL
KKALVKLRKD ILYLEEVLLE KSKEHISTIM PGYTHMQKAQ PITLSHHLLA YAEMFKRDIG
RINDAYKRTD EMPLGSGALA TSTYPIDRYM VAKDLGFSKI TLNSLDSVSD RDYVIETLSA
LSLIMMHLSR FSEEIILWCT GEFNFVELDD SYSTGSSIMP QKKNPDVAEL IRGKTGRVYG
DLITLLTVMK GIPLAYNKDM QEDKEALFDA LDTVTLSLKT FAGMIKTMKI NKDNMKKSAA
LGFTNATDLA DYLVKKGSYF RDAHGIVGQI VLQCIKDNKM IEDLTLAELK EYSPTFEEDV
YDAINLYTCV EERKVIGGPS RESVKFQIKE LQEFIHQFKG DEIYD