GenomeNet

Database: UniProt
Entry: Q8GIS1
LinkDB: Q8GIS1
Original site: Q8GIS1 
ID   ARLY_SYNE7              Reviewed;         466 AA.
AC   Q8GIS1; Q31KB4;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 115.
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=Synpcc7942_2475; ORFNames=seb0051;
OS   Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)
OS   (Anacystis nidulans R2).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Holtman C.K., Socias T., Mohler B.J., Chen Y., Min H., Golden S.S.,
RA   Youderian P., Sandoval P., Gonzalez A., Salinas I.;
RT   "Synechococcus elongatus PCC7942 genome sequence, cosmid 7H1 and 2E8.";
RL   Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33912 / PCC 7942 / FACHB-805;
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., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Golden S., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABB58505.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U30252; AAN71789.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB58505.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_039755911.1; NZ_CP130602.1.
DR   AlphaFoldDB; Q8GIS1; -.
DR   SMR; Q8GIS1; -.
DR   STRING; 1140.Synpcc7942_2475; -.
DR   PaxDb; 1140-Synpcc7942_2475; -.
DR   GeneID; 76401206; -.
DR   KEGG; syf:Synpcc7942_2475; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_3_3; -.
DR   OrthoDB; 9769623at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_2475-MONOMER; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000889800; 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; 1.10.40.30; 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; Arginine biosynthesis; Cytoplasm; Lyase;
KW   Reference proteome.
FT   CHAIN           1..466
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_0000137839"
SQ   SEQUENCE   466 AA;  51852 MW;  FC7FB90A962155ED CRC64;
     MTQAAAPQPW SDRFETALHP AIVVFNASIG FDLALIEYDL TGSQAHAQML AEQDIISREE
     GEAIVAGLEQ IRSEYRTGQF QPGLDAEDVH FAVERRLTEL LGDVGKKLHT ARSRNDQVGT
     DTRLYLRDRV DHIRQQLRDY QRVLLSQAEQ HLETLIPGYT HLQRAQPLSL AHHLHAYLEM
     AERDWERLGD LRKRLNTSPL GAGALAGTTF PIDRQRTAAL LGFERIYANS LDAVSDRDSL
     VEFLAAASLI MVHLSRLAEE VILWASEEFR FVRLSDRCAT GSSIMPQKKN PDVPELVRGK
     TGRVFGHLQA LLVVLKGLPL AYNKDLQEDK EGLFDAVQTV ESCLEAMTIL FAEGLSFQPD
     RLAAAVEADF SNATDVADYL AARGVPFREA YNLVGRVVRT CLEQGKLLKD LSLAEWQALH
     PQFEADIYTA IAPQQVVAAR NSLGGTGFEQ VRSALASVRQ RLEATC
//
DBGET integrated database retrieval system