ARLY_HALS3
ID ARLY_HALS3 Reviewed; 485 AA.
AC B0R7V5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=OE_4419R;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
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; AM774415; CAP14824.1; -; Genomic_DNA.
DR RefSeq; WP_010903820.1; NC_010364.1.
DR AlphaFoldDB; B0R7V5; -.
DR SMR; B0R7V5; -.
DR EnsemblBacteria; CAP14824; CAP14824; OE_4419R.
DR GeneID; 5953385; -.
DR KEGG; hsl:OE_4419R; -.
DR HOGENOM; CLU_027272_2_3_2; -.
DR OMA; KKNPDVF; -.
DR PhylomeDB; B0R7V5; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000001321; 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; 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Lyase.
FT CHAIN 1..485
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000089085"
SQ SEQUENCE 485 AA; 48792 MW; 5C23512E63CBEA29 CRC64;
MTGGGDPVVR RDRFSGGPAR SFLSSMDGDG RIFEADLAVD RAHVVMLAEQ DVIGDEAAAA
ILGALADVEA AGFDALPPGE DVHEAIETAV VEAVGRDGGK LHTARSRNDE VAACIRYRLR
ADLLDAIEVV VALRSALADV AAAEAETVMP GFTHLQPAQP TTVAHWALSY AGTLARDTGR
LCDAYGRTNE SPLGAAAFAG TTFGVDRERT AALLGFDGVV ANAADAAASR DFLLEAVSAL
ASVAVTCSGL AADVVFFANR GFVEVSDDYA STSSIMPQKK NPDTMELVRA TAGDAVGAQQ
ALATTLQGLP RAYNRDLQRA TGHAWTAVDG VTSAVEVAAG VVATAGWPAD DLEAAAGEGF
STATGVADAL AAGGLPFRTA HEVVALAAER GCEGATLDAV AAATEAVTGE PLSAVVEPAA
VADALDPVGS VAARDSAGGP APAAVEAAVA DVRDGIDADE AALAAERASL ADAADALAAE
VSGYV
