(data stored in ACNUC9435 zone)

SWISSPROT: ARLY_RUEPO

ID   ARLY_RUEPO              Reviewed;         463 AA.
AC   Q5LXC0;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   11-DEC-2019, entry version 95.
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=SPO0332;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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}.
DR   EMBL; CP000031; AAV93650.1; -; Genomic_DNA.
DR   RefSeq; WP_011046093.1; NC_003911.12.
DR   SMR; Q5LXC0; -.
DR   STRING; 246200.SPO0332; -.
DR   PRIDE; Q5LXC0; -.
DR   EnsemblBacteria; AAV93650; AAV93650; SPO0332.
DR   KEGG; sil:SPO0332; -.
DR   eggNOG; ENOG4105CH7; Bacteria.
DR   eggNOG; COG0165; LUCA.
DR   HOGENOM; HOG000242744; -.
DR   KO; K01755; -.
DR   OMA; MPGRTHL; -.
DR   OrthoDB; 751464at2; -.
DR   BioCyc; RPOM246200:G1G48-339-MONOMER; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000001023; 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;
DR   PRODOM; Q5LXC0.
DR   SWISS-2DPAGE; Q5LXC0.
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Lyase;
KW   Reference proteome.
FT   CHAIN           1..463
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_0000240771"
SQ   SEQUENCE   463 AA;  49961 MW;  3D71F31500FB34FF CRC64;
     MTDKTSNQMW GGRFAAGPDA IMEAINASIG FDKRLAAQDI AGSRAHAAML AATGVITDSD
     AEAIREGLLT VLSEIEAGEF TFSTALEDIH MNVEARLKEI IGEPAGRLHT ARSRNDQVAT
     DFKLWVRDQF DAAEAGLLAL LRALLGQAEA GADWVMPGFT HLQTAQPVTW GHHMMAYVEM
     FGRDLSRVRD ARARMNESPL GSAALAGTSF PIDRHMTAAA LGFDRPTANS LDAVSDRDFA
     LEFLSVASIC AMHLSRFAEE LVIWSSAQFR FVTLSDRFST GSSIMPQKKN PDAAELIRAK
     VGRIFGANTA LMMVMKGLPL AYSKDMQEDK EQVFDAADNW MLALAAMEGM VRDMTANRDS
     LAAAAGSGFS TATDLADWLV RVLGLPFRDA HHVTGALVAL AESKGCDLPD LSLDEMQSAH
     AAITEDVYGV LGVENSVNSR QSYGGTAPAQ VRAQVARWKE MLA
//

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