(data stored in ACNUC7421 zone)

SWISSPROT: ARLY_LEGPC

ID   ARLY_LEGPC              Reviewed;         411 AA.
AC   A5IHA2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   11-DEC-2019, entry version 77.
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=LPC_2851;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) 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}.
DR   EMBL; CP000675; ABQ56752.1; -; Genomic_DNA.
DR   SMR; A5IHA2; -.
DR   PRIDE; A5IHA2; -.
DR   EnsemblBacteria; ABQ56752; ABQ56752; LPC_2851.
DR   KEGG; lpc:LPC_2851; -.
DR   HOGENOM; HOG000242744; -.
DR   KO; K01755; -.
DR   OMA; MPGRTHL; -.
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;
DR   PRODOM; A5IHA2.
DR   SWISS-2DPAGE; A5IHA2.
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Lyase.
FT   CHAIN           1..411
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000000493"
SQ   SEQUENCE   411 AA;  46242 MW;  1B573B9CAF1FF8E6 CRC64;
     MTNKTWGGRF KKSLDSGVNQ FNASLSFDHV LFDQDINGSQ VHVKQLAKQK ILTEVESQAI
     YSALEEIRSE IKQGQYSFNV RDEEDIHMFI EQLLIQKIGD LGKKLHTGRS RNDQVALDLR
     LYTRDKGCLI NELLTRLIDC LDDLTSKHQQ DLMPGYTHLQ QAQPVTLGAY FNAYQCMFGR
     DKSRLEDWFK RMNYSPLGAG ALAGSTLPLD REWVAESLGF AGIIPNTLDA VSDRDFVIEL
     CSVAAMIMMH LSRLCEDLIL WSTQEFNFVI LDDAFATGSS LMPNKKNPDV PELIRGKSGR
     VYGHLMAILT VMKGLPLAYN KDMQEDKEGL FDTINTIIAC LQMITPFLQS LTFNTLLMKT
     KAQSGYLDAT AILESLVMKG MPFRDAHHQV GAWIAEAIEK QCSLNELLKG G
//

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