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ARLY_SHEB2
ID   ARLY_SHEB2              Reviewed;         455 AA.
AC   B8EBF9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 65.
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=Sbal223_4010;
OS   Shewanella baltica (strain OS223).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=407976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS223;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ovchinnikova G., Brettar I., Rodrigues J., Konstantinidis K.,
RA   Tiedje J.;
RT   "Complete sequence of chromosome of Shewanella baltica OS223.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001252; ACK48483.1; -; Genomic_DNA.
DR   RefSeq; WP_012588800.1; NC_011663.1.
DR   AlphaFoldDB; B8EBF9; -.
DR   SMR; B8EBF9; -.
DR   EnsemblBacteria; ACK48483; ACK48483; Sbal223_4010.
DR   KEGG; sbp:Sbal223_4010; -.
DR   HOGENOM; CLU_027272_2_3_6; -.
DR   OMA; KKNPDVF; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000002507; 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.
FT   CHAIN           1..455
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000116343"
SQ   SEQUENCE   455 AA;  49197 MW;  BC0D2602343514A5 CRC64;
     MALWGGRFQG ETSALFKLFN DSLPVDYRLF EQDVIGSIAW ADAIASVGII SATECRDLKK
     ALNDLLVEVN GDPAIILASG AEDIHSFVES ALIAKVGDLG KKLHTGRSRN DQVATDLKLW
     CQSEGAALLA RLQSLHAELL ALAEREFDAV MPGYTHLQRA QPVTFGHWCL AYVEMYERDI
     SRLADALTRA NTCPLGSGAL AGTAYKMDRH ALAAALNFAA PTLNSLDSVS DRDHVVELCS
     TASISMMHLS RMAEDLIFFN SGEANFISLS DEVTSGSSLM PQKKNPDALE LIRGKTGRVY
     GSLVGILTTM KALPLAYNKD MQEDKEGLFD VVDSWAICLD MAALVLSGLK VNRPNALLAA
     QQGYANSTEL ADYLVSKGMP FREAHHVVGE VVVAAIAKQI PLEEFSLAEL KTFAAIIEDD
     VYPNLTIEAC LAKRDVLGGT ALPQIQQAIA AKKAR
 
 
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