ID   ARLY_MAGSA              Reviewed;         471 AA.
AC   Q2VYN2;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 96.
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=amb4489;
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=342108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(2005).
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; AP007255; BAE53293.1; -; Genomic_DNA.
DR   RefSeq; WP_011386833.1; NC_007626.1.
DR   AlphaFoldDB; Q2VYN2; -.
DR   SMR; Q2VYN2; -.
DR   STRING; 342108.amb4489; -.
DR   EnsemblBacteria; BAE53293; BAE53293; amb4489.
DR   KEGG; mag:amb4489; -.
DR   HOGENOM; CLU_027272_2_3_5; -.
DR   OMA; KKNPDVF; -.
DR   OrthoDB; 751464at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000007058; 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;
KW   Reference proteome.
FT   CHAIN           1..471
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_0000240739"
SQ   SEQUENCE   471 AA;  51174 MW;  83D13D12AF49D421 CRC64;
     MTDTDKTKAA SSMWGGRFAG GPAAIMQRIN ASIDFDKRLY AQDIRGSKAH CRMLVKQQIL
     TEADGALILD GLDKVLAEIE AGNFPFSHAL EDIHMNVESR LAELIGEAAG RLHTARSRND
     QVATDFRLWV RDAVDGMESA LKELVTALLD RAEEHAATVM PGFTHLQTAQ PVTFGHHMMA
     YVEMISRDRS RLADARRRLN ECPLGSAALA GTSFPIDREA TARDLGFAGP MRNSLDGVSD
     RDFALEFMSA SAICAVHLSR LAEELVIWTS SQFRFVTLSD AFTTGSSIMP QKRNPDAAEL
     IRAKTGRVIG DLNALLIVMK GLPLAYSKDM QDDKEPVFEV ADTMELAIAA MTGMVRDMTV
     NVDILRAAAG AGFTTATDIA DWCVRALKMP FRRAHHVAGS LVKLAEGKNC GLEDLTLAEM
     QAIEPGITEE ARSVLSVESS VNSRTSLGGT APVRVREAVA GARRRLMDEA P