ID ARLY_YERPY Reviewed; 457 AA.
AC B1JQ59;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 01-MAY-2013, entry version 36.
DE RecName: Full=Argininosuccinate lyase;
DE Short=ASAL;
DE EC=4.3.2.1;
DE AltName: Full=Arginosuccinase;
GN Name=argH; OrderedLocusNames=YPK_4087;
OS Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Yersinia.
OX NCBI_TaxID=502800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YPIII;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T.,
RA Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Challacombe J.F., Green L., Lindler L.E., Nikolich M.P.,
RA Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL Submitted (FEB-2008) 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.
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; CP000950; ACA70346.1; -; Genomic_DNA.
DR RefSeq; YP_001722799.1; NC_010465.1.
DR ProteinModelPortal; B1JQ59; -.
DR SMR; B1JQ59; 3-456.
DR STRING; 502800.YPK_4087; -.
DR EnsemblBacteria; ACA70346; ACA70346; YPK_4087.
DR GeneID; 6090620; -.
DR KEGG; ypy:YPK_4087; -.
DR PATRIC; 18665967; VBIYerPse127545_4413.
DR eggNOG; COG0165; -.
DR HOGENOM; HOG000242744; -.
DR KO; K01755; -.
DR OMA; KEGIFDA; -.
DR ProtClustDB; PRK04833; -.
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 1 457 Argininosuccinate lyase.
FT /FTId=PRO_1000089135.
SQ SEQUENCE 457 AA; 50130 MW; C63B06697633F32F CRC64;
MALWGGRFSQ AADQRFKQFN DSLRFDYRLA EQDIIGSVAW SKALVTVGVL NADEQQQLEQ
ALSVLLEEVQ ANPHAILASD AEDIHSWVET KLIDKVGDLG KKLHTGRSRN DQVATDLKLW
CKFQITELQT AVQQLQQALV MTAEANQDAV MPGYTHLQRA QPVTFAHWCL AYVEMLSRDE
SRLQDTLKRL DVSPLGCGAL AGTAYAIDRE QLAGWLGFAS ATRNSLDSVS DRDHVLELLS
DASIGMVHLS RFAEDLIFFN SGEAAFVDLS DRVTSGSSLM PQKKNPDALE LIRGKCGRVQ
GALTGMMMTL KGLPLAYNKD MQEDKEGLFD ALDTWLDCLH MAALVLDGIQ VKRPRCKEAA
EQGYANATEL ADYLVAKGVP FREAHHIVGE AVVEAIRQGK ALEALALSDL QQFSSVIGDD
VYPILALQSC LDKRVAKGGV SPQQVASAIA EAKARLF
//