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ARLY_SYNPW
ID   ARLY_SYNPW              Reviewed;         470 AA.
AC   A5GHM4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=SynWH7803_0013;
OS   Synechococcus sp. (strain WH7803).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32051;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH7803;
RG   Genoscope;
RL   Submitted (MAY-2006) 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}.
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DR   EMBL; CT971583; CAK22439.1; -; Genomic_DNA.
DR   RefSeq; WP_011931948.1; NC_009481.1.
DR   AlphaFoldDB; A5GHM4; -.
DR   SMR; A5GHM4; -.
DR   STRING; 32051.SynWH7803_0013; -.
DR   EnsemblBacteria; CAK22439; CAK22439; SynWH7803_0013.
DR   KEGG; syx:SynWH7803_0013; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_3_3; -.
DR   OMA; KKNPDVF; -.
DR   OrthoDB; 751464at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000001566; 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..470
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000000550"
SQ   SEQUENCE   470 AA;  51785 MW;  14DA5929CB9AE85D CRC64;
     MAGGVTGGGS ATWSDRFEQG LHPAIERFNA SIGFDITLLQ EDLDGSMAHA RMLAQCGVIS
     EAEADQLCGG LEQIRAEAAE GRFQPGLDDE DVHFAVERRL IALLGPVGKK LHTGRSRNDQ
     VGTDLRLWLR RRIDELIPQV KTFQRALLRQ ALSHRRTLIP GYTHLQRAQP VCLAHHLLAY
     VEMLERDRQR LEDVRKRVNV SPLGAAALAG TPVPIDRRST AAALGFDGLY ANSLDAVSDR
     DFAVEFSAAI SLVMVHLSRL GEEVIFWASE ECGFVRLSDR CATGSSLMPQ KKNPDVPELV
     RGKCGRVFGH LQGLLTMIKG LPLAYNKDFQ EDKEALFDVV STGSQCLEAM TILMDEGLSF
     REDRLEAAVA ADFSNATDVA DYLVARQVPF REAYQIVGSV VKQCLSEGVL LRDLSLERWQ
     SFHPAIESDL YDALAPRQVV AARTSEGGTG FDRVEEQLSA WSERLDLANG
 
 
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