ID   ARLY_GEOSL              Reviewed;         458 AA.
AC   Q74GT9;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 112.
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=GSU0156;
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA   Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA   Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA   Lovley D.R., Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(2003).
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; AE017180; AAR33491.1; -; Genomic_DNA.
DR   RefSeq; NP_951218.1; NC_002939.5.
DR   RefSeq; WP_010940832.1; NC_002939.5.
DR   AlphaFoldDB; Q74GT9; -.
DR   SMR; Q74GT9; -.
DR   STRING; 243231.GSU0156; -.
DR   EnsemblBacteria; AAR33491; AAR33491; GSU0156.
DR   KEGG; gsu:GSU0156; -.
DR   PATRIC; fig|243231.5.peg.157; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_3_7; -.
DR   InParanoid; Q74GT9; -.
DR   OMA; KKNPDVF; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000000577; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IBA:GO_Central.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
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..458
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_0000137773"
SQ   SEQUENCE   458 AA;  51149 MW;  F0162C8456B94D05 CRC64;
     MAHEKLWGGR FSEPTDQFVE EFTASIDFDK RLYHQDIRGS IAHARMLGKQ GILPMAEVEK
     IVAGLQEVLA RIEAGKFDFS VALEDIHMNI EARLTEKIGE AGKRLHTGRS RNDQVALDIR
     LYLRDEIVEI SAYLDMLVDS LIYQAEANLG VIMPGYTHLQ TAQPILFSHH MMAYVEMFTR
     DKGRMEDCLR RMNVLPLGAG ALAGTTFPID REHVAELLDF PGVTRNSLDS VSDRDFALEF
     MGASSILMMH LSRFSEELIL WSTSEFKFVE LTDSFCTGSS IMPQKKNPDV PELVRGKTGR
     VYGNLMALLT VMKALPLAYN KDMQEDKEPL FDTIDTVKGS LKIFADMVRE MRINAGNMRA
     AAAKGFSTAT DVADYLVRQG MPFRDAHEVV GKTVAYCIAN GKDLPDLTMD EWQGFSDKIG
     EDIFDAITLE ASVNARVATG GTALERVKAE IERAKVGR