ID ARLY_DESDG Reviewed; 460 AA.
AC Q30YB9;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 01-MAY-2013, entry version 60.
DE RecName: Full=Argininosuccinate lyase;
DE Short=ASAL;
DE EC=4.3.2.1;
DE AltName: Full=Arginosuccinase;
GN Name=argH; OrderedLocusNames=Dde_2530;
OS Desulfovibrio desulfuricans (strain G20).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=207559;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G20;
RX PubMed=21685289; DOI=10.1128/JB.05400-11;
RA Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
RA Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C.,
RA Tapia R., Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A.,
RA Lucas S., Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
RT "Complete genome sequence and updated annotation of Desulfovibrio
RT alaskensis G20.";
RL J. Bacteriol. 193:4268-4269(2011).
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; CP000112; ABB39327.1; -; Genomic_DNA.
DR RefSeq; YP_389022.1; NC_007519.1.
DR ProteinModelPortal; Q30YB9; -.
DR STRING; 207559.Dde_2530; -.
DR EnsemblBacteria; ABB39327; ABB39327; Dde_2530.
DR GeneID; 3757547; -.
DR KEGG; dde:Dde_2530; -.
DR PATRIC; 21743997; VBIDesDes50040_2500.
DR eggNOG; COG0165; -.
DR HOGENOM; HOG000242744; -.
DR KO; K01755; -.
DR OMA; EDIHTVI; -.
DR ProtClustDB; PRK00855; -.
DR BioCyc; DALA207559:GH1L-2266-MONOMER; -.
DR UniPathway; UPA00068; UER00114.
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 Gene3D; 1.10.275.10; -; 1.
DR HAMAP; MF_00006; Arg_succ_lyase; 1; -.
DR InterPro; IPR009049; Argininosuccinate_lyase.
DR InterPro; IPR003031; D_crystallin.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR000362; Fumarate_lyase.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR PANTHER; PTHR11444:SF3; PTHR11444:SF3; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-Aspartase-like; 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 1 460 Argininosuccinate lyase.
FT /FTId=PRO_0000240726.
SQ SEQUENCE 460 AA; 50975 MW; A3AFCC45AB94B3A8 CRC64;
MTAGKLWGGR FRERTAGLVE EYTESVSYDR ALYAQDIAGS KAHARMLARQ GVISAGDAGR
ITEGLEQIRK EIESGEFVWR TEMEDVHMNI ESRLTELVGD AGRRLHTGRS RNDQVALDFR
LFVSDRIRVW KNLVRGVIAA LTAQAHEHKD TLLPGCTHLQ AAQPVSLAQH LLAYAWMLRR
DYDRLEDCDR RVRICPLGAA ALAGTTYPLD PQSVAAELDM YGVFNNSMDA VSDRDFALEA
QFCGSLIMAH MSRLCEEIIL WANPNFGYIF LPDAYATGSS IMPQKKNPDV AEIMRGKTGR
VYGGLMSLLT TLKGLPMTYN RDLQEDKEPF IDTDRTVSAS LEIMAGMVEA LRFNTRRMEN
ALRAGFLNAT ELADYLVGKG VPFRDAHHIT GNAVALAEDR GKGLEDLTLE EFHSVSDLIG
EDVFAVLDYR AAVERRCTHG GTGPASVAAQ LAALQQWLSS
//
