GenomeNet

Database: UniProt
Entry: Q2S0F5_SALRD
LinkDB: Q2S0F5_SALRD
Original site: Q2S0F5_SALRD 
ID   Q2S0F5_SALRD            Unreviewed;       437 AA.
AC   Q2S0F5;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   RecName: Full=argininosuccinate lyase {ECO:0000256|ARBA:ARBA00012338};
DE            EC=4.3.2.1 {ECO:0000256|ARBA:ARBA00012338};
GN   Name=argH {ECO:0000313|EMBL:ABC44970.1};
GN   OrderedLocusNames=SRU_2221 {ECO:0000313|EMBL:ABC44970.1};
OS   Salinibacter ruber (strain DSM 13855 / M31).
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC   Salinibacter.
OX   NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC44970.1, ECO:0000313|Proteomes:UP000008674};
RN   [1] {ECO:0000313|EMBL:ABC44970.1, ECO:0000313|Proteomes:UP000008674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13855 / CECT 5946 / M31
RC   {ECO:0000313|Proteomes:UP000008674};
RX   PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA   Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H.,
RA   Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA   Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA   Legault B., Rodriguez-Valera F.;
RT   "The genome of Salinibacter ruber: convergence and gene exchange among
RT   hyperhalophilic bacteria and archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000985};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC       from L-ornithine and carbamoyl phosphate: step 3/3.
CC       {ECO:0000256|ARBA:ARBA00004941}.
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; CP000159; ABC44970.1; -; Genomic_DNA.
DR   RefSeq; WP_011404947.1; NC_007677.1.
DR   RefSeq; YP_446326.1; NC_007677.1.
DR   AlphaFoldDB; Q2S0F5; -.
DR   STRING; 309807.SRU_2221; -.
DR   EnsemblBacteria; ABC44970; ABC44970; SRU_2221.
DR   KEGG; sru:SRU_2221; -.
DR   PATRIC; fig|309807.25.peg.2314; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_0_10; -.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000008674; Chromosome.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-EC.
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   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; 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   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   Lyase {ECO:0000313|EMBL:ABC44970.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008674}.
FT   DOMAIN          36..299
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   REGION          391..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..429
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   437 AA;  47374 MW;  AA1C2A02E13FA590 CRC64;
     MTAPLWQKDA TPATDDWAHR FTVGDDYEWD RLLLPYDVRA SRAHAWGLRQ IDVLSETEWT
     RIGDALDALL DAFEAGDVTV TPEDEDCHTV IERFVTERAG AAGEKLHTGR SRNDQVLAAL
     RLYLRDALAA IGGRAAALAD ALCELATRHP DVLMPGYTHL QRAMPSTAAL WTLGYAETLA
     GDLDALRHAR RRINVSPLGS AAGYGVPVID LPREAVADRL GFRAVQTHAT AVQLSRGKHA
     LAVGHACTQV GATCNRLASD LVLFATAEFD FVDLPPEHCT GSSIMPQKQN PDVLELARAY
     HHRLAAQMQS LATGPSNLPG GYHRDLQLTK AAVLRSVEMT SDVLTALAEV VRGVTFNPER
     TRAACAPDIL ATQRALERVA EGVPFRSAYQ QAADAEPGPV DPGAVLDAYE TDGTPGQERP
     DRVRSRLDAH GDWVVTP
//
DBGET integrated database retrieval system