ID   ARLY2_RHIME             Reviewed;         488 AA.
AC   Q92VM6;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   04-NOV-2026, entry version 129.
DE   RecName: Full=Argininosuccinate lyase 2 {ECO:0000255|HAMAP-Rule:MF_00006};
DE            Short=ASAL 2 {ECO:0000255|HAMAP-Rule:MF_00006};
DE            EC=4.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00006};
DE   AltName: Full=Arginosuccinase 2 {ECO:0000255|HAMAP-Rule:MF_00006};
GN   Name=argH2 {ECO:0000255|HAMAP-Rule:MF_00006};
GN   OrderedLocusNames=RB0673; ORFNames=SMb21094;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OG   Plasmid pSymB (megaplasmid 2).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481431; DOI=10.1073/pnas.161294698;
RA   Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA   Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT   "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT   endosymbiont Sinorhizobium meliloti.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
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; AL591985; CAC49073.1; -; Genomic_DNA.
DR   PIR; A95926; A95926.
DR   RefSeq; WP_010975548.1; NC_003078.1.
DR   AlphaFoldDB; Q92VM6; -.
DR   SMR; Q92VM6; -.
DR   EnsemblBacteria; CAC49073; CAC49073; SM_b21094.
DR   KEGG; sme:SM_b21094; -.
DR   PATRIC; fig|266834.11.peg.5601; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_2_5; -.
DR   OMA; AEWVSVY; -.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000001976; Plasmid pSymB.
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; 1.20.200.10: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; Plasmid;
KW   Reference proteome.
FT   CHAIN           1..488
FT                   /note="Argininosuccinate lyase 2"
FT                   /id="PRO_0000137813"
SQ   SEQUENCE   488 AA;  53037 MW;  376898B050516832 CRC64;
     MTEPTQLWGG RFKSGPSEAL ANLSRAPRSY FRLYKEDIAG SRAHASELKR AGVLDESEFS
     AIRAALEGIE ADVGAGREEP IAADEDLHTF LERLLMARLG TLGGKLRAGR SRNDQTANNT
     RLYLRRMARE LSQGVIAIEE ALTEQASRHT ETVMPGFTHL QPAQPVVLGH HLMAHAQSLL
     RDLQRFADWD RRFDRSPLGA AALAGSGIAR RPDLSAIDLG YSAACENSID AVAARDHVAE
     FLFICSLVAV DLSRLAEEIC LWSSKQFSWV RLHDSYSTGS SIMPQKKNPD VAELTRGMSG
     TLIGNIAGFL ATMKAMPLAY NRDLAEDKRS LFETIDVLEL VLPAFAGMVG TLEFDVEKLR
     EEAPKGFTLA TEVADWLVGR DVPFAEAHEI TGAVVRFCEE RGHDLAGLTA EDLPGIDPRL
     HPEMLAALVL EKALASRNGY GATAPEKVRE QIARFETALA ECCAFAGGPI GGGAFAGAKD
     GAEEARRR
//