ID   ARLY_ALHEH              Reviewed;         468 AA.
AC   Q0A574;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Argininosuccinate lyase;
DE            Short=ASAL;
DE            EC=4.3.2.1;
DE   AltName: Full=Arginosuccinase;
GN   Name=argH; OrderedLocusNames=Mlg_2673;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: 2-(N(omega)-L-arginino)succinate = fumarate +
CC       L-arginine.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       arginine from L-ornithine and carbamoyl phosphate: step 3/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC       subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000453; ABI58013.1; -; Genomic_DNA.
DR   RefSeq; YP_743503.1; -.
DR   GeneID; 4268806; -.
DR   GenomeReviews; CP000453_GR; Mlg_2673.
DR   KEGG; aeh:Mlg_2673; -.
DR   NMPDR; fig|187272.6.peg.2550; -.
DR   HOGENOM; Q0A574; -.
DR   OMA; Q0A574; MAEDLIF.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IEA:HAMAP.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
DR   HAMAP; MF_00006; -; 1.
DR   InterPro; IPR009049; Argininosuccinate_lyase.
DR   InterPro; IPR003031; D_crystallin.
DR   InterPro; IPR000362; Fumarate_lyase.
DR   PANTHER; PTHR11444:SF3; argH; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00145; DCRYSTALLIN.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   TIGRFAMs; TIGR00838; argH; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome;
KW   Cytoplasm; Lyase.
FT   CHAIN         1    468       Argininosuccinate lyase.
FT                                /FTId=PRO_0000321426.
SQ   SEQUENCE   468 AA;  52551 MW;  E599E2159A52CC45 CRC64;
     MTDKNTSEQL WTGRFTEATD AFVEQFSASE HFDRRLYRQD IAGSMAHARM LAEVGVLTAE
     ERDRIVDGLT RIREEIEHGQ FQWSPKLEDV HMNIEKRLTD LIGEAGKKLH TGRSRNDQVA
     TDIRLWLREA IDGILDELLR LQAGLVELAE LEADTIMPGF THMQVAQPVT FGHHLLAWYE
     MLVRDQGRLE DCRKRLNQMP LGCAALAGTS FPIDREQTCS ELGFDRPTRN SLDSVSDRDF
     AIEFNAAAAL VMTHLSRMAE EVILWASPHF GFIDLPDRFC TGSSIMPQKK NPDVAELVRG
     KTARVHGNLN ALLVLMKGQP LAYNRDNQED KEPLFDTADT LRDALTAFAD MLPAMEVQRE
     ACYRAARAGF ATATDLADYL VRKGVPFRDA HEIVGRAVRY ASDEGRDLSE LELDELQQFS
     GTISEDVFEV LTLEGSVAAR NHLGGTAPAQ VRARVAEARD RLRLLMGK
//