ID ARLY_ANADE Reviewed; 467 AA. AC Q2IGX8; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 16-JUN-2009, entry version 28. DE RecName: Full=Argininosuccinate lyase; DE Short=ASAL; DE EC=4.3.2.1; DE AltName: Full=Arginosuccinase; GN Name=argH; OrderedLocusNames=Adeh_4071; OS Anaeromyxobacter dehalogenans (strain 2CP-C). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Anaeromyxobacter. OX NCBI_TaxID=290397; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., RA Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., RA Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."; RL Submitted (JAN-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; CP000251; ABC83835.1; -; Genomic_DNA. DR RefSeq; YP_467272.1; -. DR GeneID; 3888262; -. DR GenomeReviews; CP000251_GR; Adeh_4071. DR KEGG; ade:Adeh_4071; -. DR HOGENOM; Q2IGX8; -. DR OMA; Q2IGX8; MAEDLIF. DR BioCyc; ADEH290397:ADEH_4071-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 1 467 Argininosuccinate lyase. FT /FTId=PRO_0000240710. SQ SEQUENCE 467 AA; 50416 MW; A6707CE7C612F6C0 CRC64; MRANSKAKPV SRAALAGEAD PRLVALSVSI QDDGALYAED IRGSQAHVSM LAAQGIVPKA AARRIVAALD QVRAEFAAGR IRFDPALEDV HTHVERRLGE LVGKDAGYLH AGRSRNDQVA LDERLFIVGA CDRCDAALER LQRAFLGQAR AHERTILPGY THLQRAQPVS LAHHLLAYVE MFGRDRERFA EVRRRAAVSP LGSGALAGTT LPLDREAVAA RLGLAGVTHN SLDAVSDRDS AAELLFACAL AAVHLSRIGE ELVLWTTKEF GFATLSDAFA TGSSLMPQKK NPDVGELARG RAGRALGDLV ALLAILKGLP LSYNRDLQED KRPLLGGPEA LVLTADAVAG AVGTATFHAE RMEEALGSGE ALATDAAEYL VERGVPFREA HEAVGKAAAF SAREGRPMAR LTAAEWASFH RRFEKDVLRC FDARRSLKRR ELPGAPGPRA VRAELRRWEK ALGKARR //