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 08-NOV-2023, entry version 105.
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; Pseudomonadota; 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; 1.10.40.30; 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; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
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.
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
//
