ID   ARLY_BACP2              Reviewed;         457 AA.
AC   A8FG69;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   04-NOV-2026, entry version 95.
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};
GN   OrderedLocusNames=BPUM_2576;
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=315750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032;
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA   Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA   Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA   Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA   Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA   Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA   Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(2007).
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; CP000813; ABV63236.1; -; Genomic_DNA.
DR   RefSeq; WP_012010876.1; NC_009848.4.
DR   AlphaFoldDB; A8FG69; -.
DR   SMR; A8FG69; -.
DR   STRING; 315750.BPUM_2576; -.
DR   PaxDb; 315750-BPUM_2576; -.
DR   GeneID; 5621841; -.
DR   KEGG; bpu:BPUM_2576; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_3_9; -.
DR   OMA; AAAWQVM; -.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000001355; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006526; P:L-arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01359; Argininosuccinate_lyase; 1.
DR   FunFam; 1.10.275.10:FF:000002; Argininosuccinate lyase; 1.
DR   FunFam; 1.10.40.30:FF:000001; Argininosuccinate lyase; 1.
DR   FunFam; 1.20.200.10:FF:000015; argininosuccinate lyase isoform X2; 1.
DR   Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR   Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR   Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 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; IPR022761; Fumarate-Lyase-like_N.
DR   InterPro; IPR020557; Fumarate_lyase_CS.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   NCBIfam; TIGR00838; argH; 1.
DR   PANTHER; PTHR43814; ARGININOSUCCINATE LYASE; 1.
DR   PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 1.
DR   Pfam; PF14698; ASL_C2; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00145; ARGSUCLYASE.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Lyase;
KW   Reference proteome.
FT   CHAIN           1..457
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000057047"
SQ   SEQUENCE   457 AA;  51662 MW;  2F8FCCB7973A7F89 CRC64;
     MKKLWGGRFQ KTPEKWVDEF GASIHFDKQL VKEDLTGSLA HASMLNTCGI LDDEEAATIK
     DGLNKLMKKA EADELEFSVD YEDIHLNLEK MLIDEIGPLG GKLHTARSRN DQVATDMHLY
     LNNQVEHIIE LISSFQTVLV EKAEQHVETI FPGYTHLQRA QPISFAHHML AYFWMLERDK
     ARFQDSLKRI NVSPLGCGAL AGTTFPIDRE YTAELLGFDH IYENSLDGVS DRDFILEFLS
     NSSLVMMHLS RLCEEIILWC SQEFKFIELD DTYATGSSMM PQKKNPDMAE LIRGKTGRVY
     GNLMGLLTIM KGLPLTYNKD LQEDKEGMFD TVKTIAGSLQ IFTGMIQTMT VNEDVMKKAT
     KEDFSNATEV ADYLAKKGMP FREAHEIVGK LVYTCIQEGI YLSDLPFETF TEASDLFEED
     IYTVLDPYVA VEKRTSAGGT GFKQIQLALE KAKACLA
//