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ARLY_LISMO
ID   ARLY_LISMO              Reviewed;         456 AA.
AC   Q8Y5H1;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 120.
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=lmo2091;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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; AL591982; CAD00169.1; -; Genomic_DNA.
DR   PIR; AC1336; AC1336.
DR   RefSeq; NP_465615.1; NC_003210.1.
DR   RefSeq; WP_010989893.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8Y5H1; -.
DR   SMR; Q8Y5H1; -.
DR   STRING; 169963.lmo2091; -.
DR   PaxDb; Q8Y5H1; -.
DR   EnsemblBacteria; CAD00169; CAD00169; CAD00169.
DR   GeneID; 987914; -.
DR   KEGG; lmo:lmo2091; -.
DR   PATRIC; fig|169963.11.peg.2141; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_3_9; -.
DR   OMA; KKNPDVF; -.
DR   PhylomeDB; Q8Y5H1; -.
DR   BioCyc; LMON169963:LMO2091-MON; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IBA:GO_Central.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
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..456
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_0000137787"
SQ   SEQUENCE   456 AA;  50837 MW;  44354D22AC0EDC1F CRC64;
     MEKLWGGRFQ GKSEAWIDDF GASISFDQKM AKEDLAGSLA HVAMLGKCGI IPASEAAEIT
     AGLKILQEKL AFGELEFSTV NEDIHLNIEK LLHEEIGSVA GKLHTARSRN DQVATDMHLY
     LKQAVAEIIQ SLKHLRVVLV QKAELHVETI MPGYTHLQHA QPLSFAHHLL AYFGMFTRDL
     ERLEESVKRI DISPLGSAAL AGTTFPIDRA YSAELLGFSA VYENSLDGVS DRDFIIEFLS
     NSSILMMHLS RFCEELILWT SHEFQFVELT DAFSTGSSIM PQKKNPDMAE LIRGKTGRVY
     GNLFGMLTVL KGLPLAYNKD LQEDKEGMFD TLETVQTSLD IFAGMIETMK VNTEIMEEST
     QKDFSNATEL ADYLAKKGVP FREAHEIVGK LVLECTQNGI YLQDVALSHY QEINPLIEED
     IYVVLSSKTA VQKRNSYGGT GFDQIKVALE NAKKTL
 
 
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