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Database: UniProt
Entry: Q30YB9
LinkDB: Q30YB9
Original site: Q30YB9 
ID   ARLY_DESAG              Reviewed;         460 AA.
AC   Q30YB9;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   09-JUL-2014, entry version 66.
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 alaskensis (strain G20) (Desulfovibrio desulfuricans
OS   (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; KGCDLPD; -.
DR   OrthoDB; EOG6P5ZF8; -.
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: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    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
//
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