ARLY_STAAW
ID ARLY_STAAW Reviewed; 459 AA.
AC Q8NXF3;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Argininosuccinate lyase {ECO:0000255|HAMAP-Rule:MF_00006};
DE Short=ASAL {ECO:0000255|HAMAP-Rule:MF_00006};
DE EC=4.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00006};
DE AltName: Full=Arginosuccinase {ECO:0000255|HAMAP-Rule:MF_00006};
GN Name=argH {ECO:0000255|HAMAP-Rule:MF_00006}; OrderedLocusNames=MW0842;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(N(omega)-L-arginino)succinate = fumarate + L-arginine;
CC Xref=Rhea:RHEA:24020, ChEBI:CHEBI:29806, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:57472; EC=4.3.2.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00006};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 3/3. {ECO:0000255|HAMAP-
CC Rule:MF_00006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00006}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00006}.
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DR EMBL; BA000033; BAB94707.1; -; Genomic_DNA.
DR RefSeq; WP_000066067.1; NC_003923.1.
DR AlphaFoldDB; Q8NXF3; -.
DR SMR; Q8NXF3; -.
DR EnsemblBacteria; BAB94707; BAB94707; BAB94707.
DR KEGG; sam:MW0842; -.
DR HOGENOM; CLU_027272_2_3_9; -.
DR OMA; KKNPDVF; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000000418; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
DR CDD; cd01359; Argininosuccinate_lyase; 1.
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; PTHR43814; PTHR43814; 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; Cytoplasm; Lyase.
FT CHAIN 1..459
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137826"
SQ SEQUENCE 459 AA; 52016 MW; DF3BE691AD786B77 CRC64;
MSNKAWGGRF EVQPEEWVDD FNASITFDQT LINQDIEGSI 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
