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Database: UniProt
Entry: W7CH86_9LIST
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ID   W7CH86_9LIST            Unreviewed;       458 AA.
AC   W7CH86;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Argininosuccinate lyase {ECO:0000256|ARBA:ARBA00012338, ECO:0000256|HAMAP-Rule:MF_00006};
DE            Short=ASAL {ECO:0000256|HAMAP-Rule:MF_00006};
DE            EC=4.3.2.1 {ECO:0000256|ARBA:ARBA00012338, ECO:0000256|HAMAP-Rule:MF_00006};
DE   AltName: Full=Arginosuccinase {ECO:0000256|HAMAP-Rule:MF_00006};
GN   Name=argH {ECO:0000256|HAMAP-Rule:MF_00006};
GN   ORFNames=PCORN_02791 {ECO:0000313|EMBL:EUJ32263.1};
OS   Listeria cornellensis FSL F6-0969.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1265820 {ECO:0000313|EMBL:EUJ32263.1, ECO:0000313|Proteomes:UP000019254};
RN   [1] {ECO:0000313|EMBL:EUJ32263.1, ECO:0000313|Proteomes:UP000019254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL F6-969 {ECO:0000313|Proteomes:UP000019254};
RX   PubMed=24599893; DOI=10.1099/ijs.0.052720-0;
RA   den Bakker H.C., Warchocki S., Wright E.M., Allred A.F., Ahlstrom C.,
RA   Manuel C.S., Stasiewicz M.J., Burrell A., Roof S., Strawn L., Fortes E.D.,
RA   Nightingale K.K., Kephart D., Wiedmann M.;
RT   "Listeria floridensis sp. nov., Listeria aquatica sp. nov., Listeria
RT   cornellensis sp. nov., Listeria riparia sp. nov. and Listeria grandensis
RT   sp. nov., from agricultural and natural environments.";
RL   Int. J. Syst. Evol. Microbiol. 64:1882-1889(2014).
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000985, ECO:0000256|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.
CC       {ECO:0000256|ARBA:ARBA00004941, ECO:0000256|HAMAP-Rule:MF_00006}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00006}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EUJ32263.1}.
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DR   EMBL; AODE01000006; EUJ32263.1; -; Genomic_DNA.
DR   RefSeq; WP_036077209.1; NZ_AODE01000006.1.
DR   AlphaFoldDB; W7CH86; -.
DR   STRING; 1265820.PCORN_02791; -.
DR   PATRIC; fig|1265820.5.peg.546; -.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000019254; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00006};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW   Rule:MF_00006}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00006}.
FT   DOMAIN          7..301
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          364..431
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   458 AA;  50553 MW;  BC8843B8517A9E7F CRC64;
     MEKLWGGRFQ GKSEAWIDEF GASIFFDAKL AKQDIAGSLA HVAMLGKCGI ISADEAAQIM
     AGLEVLAGKL AAGELEFSVV NEDIHLNIEK LLHEEIGPVA GKLHTARSRN DQVATDMHLY
     LKEAVTEIIA SLAHLRTVLV TKAEDHVETI MPGYTHLQHA QPISFAHHLL AYYGMFSRDL
     ERLTESVKRI DISPLGCAAL AGTTFPIDRA YSAEQLGFSA MYDNSLDGVS DRDFIIEFLS
     NSALLMTHLS RFCEELILWT SHEFQFVELI DAFATGSSIM PQKKNPDMAE LIRGKTGRVY
     GNLFGLLTVL KGLPLAYNKD LQEDKEGMFD TVHTVKTSLD IFAGMIETMK VNTSVMEQAT
     QKDFSNATEL ADYLAKKGVP FREAHEIVGK LVLACTQKGI YLQDVALADY QAIQPVIEQD
     IYDALASYTA VAKRNSYGGT GFDQIRAMIE KAKKNTIN
//
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