ARLY_SYNS3
ID ARLY_SYNS3 Reviewed; 472 AA.
AC Q0IE70;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=sync_0013;
OS Synechococcus sp. (strain CC9311).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=64471;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9311;
RX PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA Paulsen I.T.;
RT "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT coastal environment.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
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; CP000435; ABI46333.1; -; Genomic_DNA.
DR RefSeq; WP_011618004.1; NC_008319.1.
DR AlphaFoldDB; Q0IE70; -.
DR SMR; Q0IE70; -.
DR STRING; 64471.sync_0013; -.
DR PRIDE; Q0IE70; -.
DR EnsemblBacteria; ABI46333; ABI46333; sync_0013.
DR KEGG; syg:sync_0013; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_3; -.
DR OMA; KKNPDVF; -.
DR OrthoDB; 751464at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000001961; 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..472
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000000551"
SQ SEQUENCE 472 AA; 52082 MW; F9D99C5C54F90307 CRC64;
MAGGVTGGGS ATWSDRFEQG LHPAIERFNA SIGFDITLLQ EDLDGSIAHA RMLADCGVIQ
VEEADQLVGG LEQVRQEAAS GLFQPGLADE DVHFAVERRL IALLGPVGKK LHTGRSRNDQ
VGTDLRLWLR RRLDELEQHL LGFQRALLDQ ANLHSNTLIP GYTHLQRAQP LCLAHHLLAY
VEMVERDRQR MADLRKRLNL SPLGAAALAG TPVPIDRRST ASALGFDGIY ANSLDAVSDR
DFTVEFSAAA SLVMVHLSRL AEEVIFWASE ECGFVRLTDR CATGSSLMPQ KKNPDVPELV
RGKCGRVFGH LQGLLTMIKG LPLAYNKDFQ EDKEALFDVV ATTSQCLEAM TILLQEGLSF
RTERLEAAVA ADYSNATDVA DYLVAKQVPF REAYQLVGAV VKHCLQEGVL LRELTLERWQ
QFHPAIEADL FEALTPRNVV AARTSEGGTG FDRVNEQLAI WNQRFGLADQ VF
