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ARLY_SYNSC
ID   ARLY_SYNSC              Reviewed;         472 AA.
AC   Q3ANN7;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
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=Syncc9605_0013;
OS   Synechococcus sp. (strain CC9605).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=110662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9605;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9605.";
RL   Submitted (JUL-2005) 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; CP000110; ABB33795.1; -; Genomic_DNA.
DR   RefSeq; WP_011363057.1; NC_007516.1.
DR   AlphaFoldDB; Q3ANN7; -.
DR   SMR; Q3ANN7; -.
DR   STRING; 110662.Syncc9605_0013; -.
DR   EnsemblBacteria; ABB33795; ABB33795; Syncc9605_0013.
DR   KEGG; syd:Syncc9605_0013; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_3_3; -.
DR   OMA; KKNPDVF; -.
DR   OrthoDB; 751464at2; -.
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..472
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_0000240780"
SQ   SEQUENCE   472 AA;  52271 MW;  11092AF4E1719277 CRC64;
     MAGGVTGGAA GTWSDRFEQG LHPFIEAFNA SIGFDLTLLQ EDLDGSIAHA RMLASVGVIT
     EAEAEQLVEG LETVRAEAAS GSFQPGLADE DVHFAVERRL IALLGPVGKK LHTGRSRNDQ
     VGTDLRLWLR RRLDGLDQDL QRLQGALLTQ ADRHRRTMIP GYTHLQRAQP LCLAHHLLAY
     VEMLERDRER LQDARKRVNI CPLGAAALAG TPVPIDRQRT AKELGFSAVY ANSLDAVSDR
     DFCVEFSAAA SLVMVHLSRL AEEVIAWASE EFGFVRLSDR CATGSSLMPQ KKNPDVPELV
     RGKTGRVFGH LQGLLTMIKG LPLAYNKDFQ EDKEALFDAF RTTRDCVEAM AILFEEGLDF
     RVERLNEAVE QDFSNATDVA DYLVSRGVPF REAYQLVGAV VRRCLEQGCL LRDLDLSAWK
     ELHPAFEADL HDALAPRAVV AARRSEGGTG FERVDEQLQR WLQRFNGTQP VG
 
 
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