ID   ARLY_RHOPB              Reviewed;         465 AA.
AC   Q20WT9;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   25-MAY-2022, entry version 89.
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=RPC_4875;
OS   Rhodopseudomonas palustris (strain BisB18).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316056;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB18;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABD90397.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000301; ABD90397.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041803284.1; NC_007925.1.
DR   AlphaFoldDB; Q20WT9; -.
DR   SMR; Q20WT9; -.
DR   STRING; 316056.RPC_4875; -.
DR   EnsemblBacteria; ABD90397; ABD90397; RPC_4875.
DR   KEGG; rpc:RPC_4875; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_3_5; -.
DR   OrthoDB; 751464at2; -.
DR   UniPathway; UPA00068; UER00114.
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.
FT   CHAIN           1..465
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_0000240762"
SQ   SEQUENCE   465 AA;  50413 MW;  DD49CFDDC41CC2AD CRC64;
     MSNKMWGGRF SERPDAIMEE INVSIDVDRH LYAQDIAASK AHAAMLAAQG IVTAKDAKNI
     AKGLDTILSE IVAGSFDFKR ALEDIHMNVE SRLSELIGPA AGRLHTARSR NDQVATDFRL
     FVRDTIDGID AALASYQHAL ATRALEHADT VMPGFTHLQT AQPVTFGHHL MAYVEMAARD
     RGRFRDARKR LNESPLGAAA LAGTSFPIDR DATAKALGFE RPMANSLDAV SDRDFVLETL
     AAASIAAVHL SRFAEEIVLW TSPLVGMVRL SDKFTTGSSI MPQKRNPDAA ELARAKTGRV
     IGALTGLLIV MKGLPLAYQK DMQEDKQGAM EAFAALSLAI RAMSGMVSDL VPDPARMKQA
     AGEGYATATD LADWLVRELK MPFRDAHHVT GRIVGEASKQ GVALHELPLA EMQAIEPRIT
     QQALSVLSVE SSVKSRVSYG GTAPKNVRAQ AKAWLKRLEK EHNSG