ID   ARLY_ALCBS              Reviewed;         464 AA.
AC   Q0VM25;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Argininosuccinate lyase;
DE            Short=ASAL;
DE            EC=4.3.2.1;
DE   AltName: Full=Arginosuccinase;
GN   Name=argH; OrderedLocusNames=ABO_2325;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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.
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DR   EMBL; AM286690; CAL17773.1; -; Genomic_DNA.
DR   RefSeq; YP_694045.1; -.
DR   GeneID; 4213482; -.
DR   GenomeReviews; AM286690_GR; ABO_2325.
DR   KEGG; abo:ABO_2325; -.
DR   NMPDR; fig|393595.12.peg.2326; -.
DR   HOGENOM; Q0VM25; -.
DR   OMA; Q0VM25; ATDTRLY.
DR   BioCyc; ABOR393595:ABO_2325-MON; -.
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    464       Argininosuccinate lyase.
FT                                /FTId=PRO_1000000450.
SQ   SEQUENCE   464 AA;  52247 MW;  AA9D7479ED61EAF2 CRC64;
     MTDKQQNKLW GGRFSESTDQ FVQEFTASVN FDRRMYRQDI YGSQAHATML AEVGVLTDEE
     RDAIIVGLRE IQLEIENGEF QWSVALEDVH MNIEARLTDK IGITGKKLHT GRSRNDQVAT
     DIRLWLRDEL LILEEQFLHL MQGLLNLAER EAATIMPGFT HLQTAQPVTF GHHLLAWFEM
     LKRDRERLLD CKKRVNRMPL GAAALAGTTY PINRERTCEL LGFDGVCENS LDAVSDRDFA
     IEFCAMAALT MTHLSRISEE LVLWTSAQFN FINLPDRFCT GSSIMPQKKN PDVPELVRGK
     TGRVNGHLIS LLTLMKSQPL AYNKDNQEDK EPLYDAVDTL KGSLRAFGDM IPALEPNREV
     MREAARRGFA TATDLADYLV RKGIAFRDSH EIVGKAVAYG VEKKKDLGDM SLSELKQFSD
     QIEDNVFEVL TLEGSVSARN HIGGTAPDQV RAAVARAREA LDNT
//