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Database: UniProt
Entry: A9BIA3
LinkDB: A9BIA3
Original site: A9BIA3 
ID   ARLY_PETMO              Reviewed;         441 AA.
AC   A9BIA3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   11-JUN-2014, entry version 44.
DE   RecName: Full=Argininosuccinate lyase;
DE            Short=ASAL;
DE            EC=4.3.2.1;
DE   AltName: Full=Arginosuccinase;
GN   Name=argH; OrderedLocusNames=Pmob_1701;
OS   Petrotoga mobilis (strain DSM 10674 / SJ95).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Petrotoga.
OX   NCBI_TaxID=403833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10674 / SJ95;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Meincke L., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Noll K., Richardson P.;
RT   "Complete sequence of Petroga mobilis SJ95.";
RL   Submitted (NOV-2007) 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 (By similarity).
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC       subfamily.
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DR   EMBL; CP000879; ABX32394.1; -; Genomic_DNA.
DR   RefSeq; YP_001568717.1; NC_010003.1.
DR   ProteinModelPortal; A9BIA3; -.
DR   STRING; 403833.Pmob_1701; -.
DR   EnsemblBacteria; ABX32394; ABX32394; Pmob_1701.
DR   GeneID; 5757416; -.
DR   KEGG; pmo:Pmob_1701; -.
DR   PATRIC; 22921226; VBIPetMob40494_1827.
DR   eggNOG; COG0165; -.
DR   HOGENOM; HOG000242744; -.
DR   KO; K01755; -.
DR   OMA; KEGIFDA; -.
DR   OrthoDB; EOG6P5ZF8; -.
DR   BioCyc; PMOB403833:GH51-1746-MONOMER; -.
DR   UniPathway; UPA00068; UER00114.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
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; PTHR11444; PTHR11444; 1.
DR   PANTHER; PTHR11444:SF3; PTHR11444:SF3; 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; Complete proteome;
KW   Cytoplasm; Lyase.
FT   CHAIN         1    441       Argininosuccinate lyase.
FT                                /FTId=PRO_1000073852.
SQ   SEQUENCE   441 AA;  50502 MW;  9517924FED800FF0 CRC64;
     MKLWGGRFKE KIAEDMEIFN SSINVDIRLL PYDIEASLAH AEGLKKAKII SEEEFEQIER
     ALREIKEEKF EEIPKVEDVH TLVEQMLVEK IGDVGKKIHT ARSRNDQIAT DERMYLRNEI
     FKIIDLLEQL NVVLVELSKK YKNKIMPGYT HMQRAQPITF SHHLLAYVEM FKRDIDRLKD
     SLKRVNVSVL GSGALAGTSY DIDRTYVASL LGFNEVSLNS IDGVSDRDFI VEFLSIASLI
     MMHLSRFSEE IVLWSSQEFN FVELSDEYST GSSIMPQKKN PDSAELIRGK TGRVYGNLLS
     LLTTMKGLPL AYNKDMQEDK EPLFDTVDTL KVCLKVFIGM LKTMSVNEEK MKQAVKFGYL
     NATDLADYLV KKGIPFRNAH DIVGKLVAYA ITKKVPIEEL NISEFKNFCQ SIDEDVYEVL
     NIKNILKSRK TIGAARWEED V
//
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