ARLY_LEPBL
ID ARLY_LEPBL Reviewed; 470 AA.
AC Q052A1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=LBL_1352;
OS Leptospira borgpetersenii serovar Hardjo-bovis (strain L550).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=355276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L550;
RX PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA Rood J.I., Davies J.K., Adler B.;
RT "Genome reduction in Leptospira borgpetersenii reflects limited
RT transmission potential.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(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}.
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DR EMBL; CP000348; ABJ78844.1; -; Genomic_DNA.
DR RefSeq; WP_011670061.1; NC_008508.1.
DR AlphaFoldDB; Q052A1; -.
DR SMR; Q052A1; -.
DR KEGG; lbl:LBL_1352; -.
DR PATRIC; fig|355276.3.peg.1716; -.
DR HOGENOM; CLU_027272_2_3_12; -.
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..470
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000000495"
SQ SEQUENCE 470 AA; 53145 MW; F804BBA59719A09C CRC64;
MTGKEKKLWG GRFQEKPSSI LERIGESVSF DHKLYKEDIQ GSIAHARMLK QIGILSGDEL
SKIETSLLQI KTELEEGKLE FKSELEDIHM HIESRLTELI GETGKKLHTA RSRNDQVTQD
VRLYILGRGK EILKSIVSLR FSLYEKAKRS VDVIIPGYTH LQVAQPIRAS QYLLSWFWAL
ERDQEFFRFA LKASDELALG GGAMAGVNYA TDREFLKKEL GLSKVSPNSM DGVSSRDHIL
EFLFACTQLM IHASRICEDI ILYSSQEFGI LKLSDSLTTG SSIMPQKKNP DIAELIRGKA
GRVIGNLNHL LVMLKGLPST YNRDLQEDKL ALFDSVETVE ISLEGIREMI EDWVWVPERA
ESSLKNGFAT ATDLADFLVY EKKVPFRTAH ELVGTLVRVC VEQKRTLFDL PEPDRIAVSE
HFVGKEYENA VSLSLSADKK ISYGGTSKKR QEEQLKIALE SLKQTETLFL
