ID ARLY_CLOTE Reviewed; 438 AA.
AC P59616;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 1.
DT 27-MAR-2024, 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=CTC_00562;
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88;
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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; AE015927; AAO35181.1; -; Genomic_DNA.
DR RefSeq; WP_011098847.1; NC_004557.1.
DR AlphaFoldDB; P59616; -.
DR SMR; P59616; -.
DR STRING; 212717.CTC_00562; -.
DR GeneID; 24254794; -.
DR KEGG; ctc:CTC_00562; -.
DR HOGENOM; CLU_027272_2_3_9; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000001412; 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; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 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 NCBIfam; TIGR00838; argH; 1.
DR PANTHER; PTHR43814; ARGININOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 1.
DR Pfam; PF14698; ASL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 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_0000137761"
SQ SEQUENCE 438 AA; 50297 MW; 97CCED1E27807C53 CRC64;
MKLWGGRFKG EENKLMEDFN SSLSFDKRLY KEDILGSKAH VKMLGNCNIL KDYEVEEIIK
GLDSILKDIE DDKLKIQGEY EDIHSFIESN LIQRIGDVGK KLHTARSRND QVAVDFKLYA
KNISLKIIES IETLQNTIKN LAEKNNVIMP GYTHLQRAQV VTFKHHIMAY YNMLKRDKKR
IENSIENMDE SPLGCCALAG TTYETDRKFT AKKLGFRKEV DNFLDGVSDR DFVIEFISDF
SIIMMHLSRL SEELILWSSK EFDFIEISDE FSTGSSIMPQ KKNPDAAELI RGKTGRVYGD
LIAILTVMKG IPLAYNKDMQ EDKESFFDAS DTVLSCIKVM EGMLSSLKVK KGNTLRAVKM
GFLNATESAD YLVLKGVPFR DAHKIIGEIV LYCEEKDKSI EELNINELKK FSTFFNEDIY
EFIDYENALN RGIKKEIK
//
