ID   ARLY_ACIBT              Reviewed;         477 AA.
AC   A3M1E0; A3M1D9;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2015, sequence version 2.
DT   25-MAY-2022, entry version 100.
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};
GN   OrderedLocusNames=A1S_0258, A1S_0259;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC
OS   KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by high-
RT   density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
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=ABO10733.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=ABO10734.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=ABO10734.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CP000521; ABO10734.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP000521; ABO10733.1; ALT_FRAME; Genomic_DNA.
DR   RefSeq; WP_000213740.1; NZ_CP053098.1.
DR   AlphaFoldDB; A3M1E0; -.
DR   SMR; A3M1E0; -.
DR   GeneID; 66398756; -.
DR   KEGG; acb:A1S_0258; -.
DR   KEGG; acb:A1S_0259; -.
DR   HOGENOM; CLU_3338910_0_0_6; -.
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..477
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_0000434563"
SQ   SEQUENCE   477 AA;  52735 MW;  E64770F4FF92A13D CRC64;
     MTTSSNPPNS AAPNQTSGMW GGRFSEATDA FVAEFTASVQ FDQRFYKQDI AGSIAHATML
     AKVGVLTEAE RDDIIEGLST IRAEIEAGTF EWRIDLEDVH MNIESRLTQR IGITGKKLHT
     GRSRNDQVAT DIRLYLRDEI DDILGLLERL QKGLLGLAAK NVNTIMPGFT HLQTAQPVTF
     GHHLLAWFEM LVRDTERLQD CRKRVNRMPL GSAALAGTTY PIDRAYTAEL LGFEAVSENS
     LDAVSDRDFA IEFNAAASLI MMHLSRMSEE LILWTSAQFK FVNIPDRFCT GSSIMPQKKN
     PDVPELIRGK SGRVFGDLIS LLTLMKGQPL AYNKDNQEDK EPLFDAIDTV RGSLMAFADM
     IPALVPNVEI MREAALRGFS TATDLADYLV KKGVAFRDAH EIVGKAVALG VAEEKDLSEL
     TLEQLQQFSD LITADVFDKA LTLEASVNAR DHIGGTSPKQ VEAAIARAHK RLEQLYA