ID   ARLY_BORA1              Reviewed;         470 AA.
AC   Q2L1J6;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-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=BAV1635;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(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; AM167904; CAJ49244.1; -; Genomic_DNA.
DR   RefSeq; YP_786155.1; -.
DR   GeneID; 6265535; -.
DR   GenomeReviews; AM167904_GR; BAV1635.
DR   KEGG; bav:BAV1635; -.
DR   NMPDR; fig|521.1.peg.1773; -.
DR   HOGENOM; Q2L1J6; -.
DR   OMA; Q2L1J6; 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    470       Argininosuccinate lyase.
FT                                /FTId=PRO_0000240715.
SQ   SEQUENCE   470 AA;  51763 MW;  5DC0E12724EB3626 CRC64;
     MANTPSQQDQ FANKAQAWSA RFSEPVSDLV KRYTASVDFD KRLARHDIRG SLAHADMLAA
     QGIISAQDLA DIERGMQQIL SEIDAGSFQW LLDLEDVHLN IEKRLVELVG DAGKRLHTGR
     SRNDQVATDI RLWLRDEIDL LIDLLRQLRH ALATVALDNA GTIMPGFTHL QVAQPVTFGH
     HLLAYAEMFG RDAERLADCR KRVNRLPLGA AALAGTSYPI DRERVASTLG FDGVCRNSLD
     AVSDRDFAIE FCAAASLIMT HVSRLSEELV LWMSPRVGFI DLADRFCTGS SIMPQKKNPD
     VPELARGKTG RVNGHLVALL TLMKGQPLAY NKDNQEDKEG LFDTADTLRD TLTIFADMAG
     GIKVKADNMR AAALQGFATA TDLADYLVKR GLPFRDAHEV VAHAVRDCEQ RGCDLADLSL
     AELQAYHPSI EADIHQVLTL EGSVAARKHT GGTAPERVRE EAQRVIQETA
//