ARLY_LEPBP
ID ARLY_LEPBP Reviewed; 478 AA.
AC B0SR12;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=LEPBI_I1606;
OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=456481;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Patoc 1 / ATCC 23582 / Paris;
RX PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL PLoS ONE 3:E1607-E1607(2008).
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; CP000786; ABZ97713.1; -; Genomic_DNA.
DR RefSeq; WP_012388591.1; NC_010602.1.
DR AlphaFoldDB; B0SR12; -.
DR SMR; B0SR12; -.
DR STRING; 456481.LEPBI_I1606; -.
DR KEGG; lbi:LEPBI_I1606; -.
DR HOGENOM; CLU_027272_2_3_12; -.
DR OMA; KKNPDVF; -.
DR OrthoDB; 751464at2; -.
DR BioCyc; LBIF456481:LEPBI_RS07925-MON; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000001847; Chromosome I.
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..478
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000089090"
SQ SEQUENCE 478 AA; 54370 MW; BB3102B9316E5AAE CRC64;
MKEKKLWGGR FDAAPSSLMI RIGESISFDQ ELYRHDIEGS ISHSRMLRRI GILSESEQRK
IETGLGQIKK EIDSGKFEFK IENEDIHMSI ESRLTELLGD LGKKLHTGRS RNDQVSQDVR
LYIKSEMHSI LILVYDLLTV WLKKAEAHTK TIIPGYTHLQ IAQPIRASHY FLSHFWANVR
DFEDFYSAFE RADELVLGSG ALAGVNYETD REYLRKDLNL ARMSENSMDA VSQRDHIFKF
LFASSQFMVH ASRFCEEIIL YTSQEFSYFK LPDHLTTGSS IMPQKKNPDV AELIRGKAGR
VIGNLTHLLV MLKGTPLSYN RDFQEDKIPL FDTVKQIKIC TEGIRDMVEG IQIFPENATR
SLRNGFSTAT DLADWLVSAK GIPFRSAHEI VGELVKHCSM KGYDLFTIPS GERGQIHAVL
TDPGYEAAIS LETSCDKKDV FGGTALPRQK EQIKRAKAKL NELTKKLKQI ESKGKKTI