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ARLY_DESAL
ID   ARLY_DESAL              Reviewed;         465 AA.
AC   B8FH31;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=Dalk_0410;
OS   Desulfatibacillum aliphaticivorans.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfatibacillum.
OX   NCBI_TaxID=218208;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK-01;
RX   PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA   Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA   Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT   "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT   for anaerobic alkane oxidation.";
RL   Environ. Microbiol. 14:101-113(2012).
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; CP001322; ACL02119.1; -; Genomic_DNA.
DR   RefSeq; WP_012609559.1; NC_011768.1.
DR   AlphaFoldDB; B8FH31; -.
DR   SMR; B8FH31; -.
DR   PRIDE; B8FH31; -.
DR   EnsemblBacteria; ACL02119; ACL02119; Dalk_0410.
DR   KEGG; dal:Dalk_0410; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_3_7; -.
DR   OMA; KKNPDVF; -.
DR   OrthoDB; 751464at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000000739; Chromosome.
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;
KW   Reference proteome.
FT   CHAIN           1..465
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000116202"
SQ   SEQUENCE   465 AA;  52126 MW;  F8AA861705FC9923 CRC64;
     MAEHKPWDGR FAEKTDDMVE AFTSSIQVDK RLYAHDITGS IAHARTLAEA GVITSDEADA
     MEKGLRQVKG EIEAGNFKYD DSLEDIHMHI ESRLTEILGP TAAKLHTGRS RNDQIALDNR
     LYLRDETRRI IAMLHELRQA IVDSAQAHLD YFVPGYTHLQ RAQPVLLSHH LMAYYEMFTR
     DSDRFTDALY RINVMPLGSA ALAGTTFPLD REYTASLLGF EGVTQNSMDA VSDRDFIMEF
     LSDASICMVH LSRMSEELVL WSSSEFAFLN MPDAFATGSS IMPQKKNPDV PELVRGKTGR
     VVGSLMAILT TMKSLPMAYN RDMQEDKPPL FDAVDTLKAC VAMFARMVPK LEFNRRNMFD
     ASNQGFLNAT DMADYLVEKG VPFREAHGIV GRAVAYALDR GRELHEISLN DLRKFSDKLE
     KDLYEALTVE HVVERRRTIG GTASVNVIAA IGRAQTQLQA ETSGD
 
 
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