ID   ARLY2_RHILO             Reviewed;         927 AA.
AC   Q981V0;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Argininosuccinate lyase 2;
DE            Short=ASAL 2;
DE            EC=4.3.2.1;
DE   AltName: Full=Arginosuccinase 2;
GN   Name=argH2; OrderedLocusNames=mll9226;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OG   Plasmid pMLa.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC       from L-ornithine and carbamoyl phosphate: step 3/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the lyase 1 family.
CC       Argininosuccinate lyase subfamily. {ECO:0000305}.
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DR   EMBL; BA000013; BAB54609.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q981V0; -.
DR   SMR; Q981V0; -.
DR   EnsemblBacteria; BAB54609; BAB54609; BAB54609.
DR   KEGG; mlo:mll9226; -.
DR   HOGENOM; CLU_332539_0_0_5; -.
DR   OMA; YAFGPAH; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000000552; Plasmid pMLa.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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   InterPro; IPR009049; Argininosuccinate_lyase.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR003806; ATP-grasp_PylC-type.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
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; PF02655; ATP-grasp_3; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Lyase; Plasmid.
FT   CHAIN           1..927
FT                   /note="Argininosuccinate lyase 2"
FT                   /id="PRO_0000137811"
FT   DOMAIN          135..333
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   REGION          431..927
FT                   /note="Argininosuccinate lyase"
SQ   SEQUENCE   927 AA;  99126 MW;  64E4255459968AB5 CRC64;
     MEPIPLEAEK PGSCPEPFGG SLMNRGSFLF VESNTTGTGE LLMKRARLLG FETYLVTRNP
     ARYPFLRDSV AQLIEAETRS PDELVGVATK LSGLAGIYSS SDYFVEAASS AAMAMGLPAA
     NARAIATCRN KWKQATELQR HSIPIPETWL ATSIRDVENI LAHGTLPVVV KPVSGSGSSG
     VRLCDSAAAA IAGFNSAKSV LQDQVDLPSP DILIQQYVEG KEYSAEIIAY DGKLHCLGIL
     AKHKGPPPCF VEVGHDFPAP LLEPSLQELA SFASGAVSAL GLEFGPAHVE FVITESGPVI
     IEVNPRLAGG MIPVMLSHAL GTSILDMVIR LYAGEGFTPP RGSARAGAIR FRLAPTSGKL
     KSLGFSRNPD PTVPEAGLLK SEGGDVQIKG DFRDRVAYAV GVADELDAAA AAADRMIDSL
     VIDIETAADE SDKQDPGPGE GRWALHPEAM KLLAPPIEIS RDGRLLQHQA AIDEAHLVML
     ADQGLVSQAA AADLLKHILD LQDEGFQSLE GRDAPRGVYL AYEAELAARA GPEKAGWLHL
     ARSRNDLNAT ISLLVLREAA CSISQQIGIA QGALLQRVEE ASSLVAPLYS QYQIALPGSP
     GHYLLGVFFA LGRERQRLHS LLEDIRNCPM GAGAGGGTSM PIDPLKTASL LGFEEPSFNS
     LDAVASRDHH LHGLSIFASI STLLSRVAQD LQVWTTREFA LIDVPRNLAG GSSMLPQKKN
     PFLLEHIKGS ASTVIGAYVS AATATCKAPF SNSIEVSNYG CSPLRLSEEA LQRALILTSL
     IVKGMSFNVR SMRDHLEDGS SMTAIAAERM ASRGIPFREA HTQIGEIAQR LSQDDCATQR
     RSELASQLAG VFPVSLEECR DALQFGGGPG KRSTDDQLSV AKTHFREMEL KCAEISERWA
     HAEAHCKGRV KELIDKHRST CRSGVCG