ID D0K3M8_STAAD Unreviewed; 459 AA.
AC D0K3M8;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 01-MAY-2013, entry version 27.
DE RecName: Full=Argininosuccinate lyase;
DE Short=ASAL;
DE EC=4.3.2.1;
DE AltName: Full=Arginosuccinase;
GN Name=argH; OrderedLocusNames=SAAV_0921;
OS Staphylococcus aureus (strain ED98).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX NCBI_TaxID=681288;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ED98;
RX PubMed=19884497; DOI=10.1073/pnas.0909285106;
RA Lowder B.V., Guinane C.M., Ben Zakour N.L., Weinert L.A.,
RA Conway-Morris A., Cartwright R.A., Simpson A.J., Rambaut A.,
RA Nuebel U., Fitzgerald J.R.;
RT "Recent human-to-poultry host jump, adaptation, and pandemic spread of
RT Staphylococcus aureus.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19545-19550(2009).
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; CP001781; ACY10838.1; -; Genomic_DNA.
DR RefSeq; YP_003281844.1; NC_013450.1.
DR ProteinModelPortal; D0K3M8; -.
DR SMR; D0K3M8; 6-457.
DR STRING; 681288.SAAV_0921; -.
DR EnsemblBacteria; ACY10838; ACY10838; SAAV_0921.
DR GeneID; 8613679; -.
DR KEGG; sad:SAAV_0921; -.
DR PATRIC; 32445894; VBIStaAur139507_0925.
DR eggNOG; COG0165; -.
DR HOGENOM; HOG000242744; -.
DR KO; K01755; -.
DR OMA; KEGIFDA; -.
DR BioCyc; SAUR681288:GJ8Z-912-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.
SQ SEQUENCE 459 AA; 52017 MW; 6C6A89026336228C CRC64;
MSNKAWGGRF EVQPEEWVDD FNASITFDQT LIDQDIEGSI AHATMLANQG IISQQDSEQI
IQGLKSIQHD YHQDQIQFSA SLEDIHLNIE HELIKRIGDA GGKLHTGRSR NDQVATDMHL
YTKKQVQDII ALIKSLQSVI VDIASNNVDT IMPGYTHLQR AQPISFAHHI MTYFWMLQRD
QQRFEDSLKR IDINPLGAAA LSGTTYPIDR HETTALLNFG SLYENSLDAV SDRDYIIETL
HNISLTMVHL SRFAEEIIFW STDEAKFITL SDAFSTGSSI MPQKKNPDMA ELIRGKVGRT
TGHLMSMLMT LKGLPLAYNK DMQEDKEGLF DAVHTIKGSL RIFEGMIQTM TINKERLNQT
VKEDFSNATE LADYLVTKNI PFRTAHEIVG KIVLECIQQG HYLLDVPLAT YQQHHSSIDA
DIYDYLQPEN CLKRRQSYGS TGQSSVKQQL DVAKQLLSQ
//
