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ARLY_PYRCJ
ID   ARLY_PYRCJ              Reviewed;         429 AA.
AC   A3MT36;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=Pcal_0368;
OS   Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=410359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21063 / JCM 11548 / VA1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA   Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL   Submitted (FEB-2007) 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; CP000561; ABO07803.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3MT36; -.
DR   SMR; A3MT36; -.
DR   STRING; 410359.Pcal_0368; -.
DR   EnsemblBacteria; ABO07803; ABO07803; Pcal_0368.
DR   KEGG; pcl:Pcal_0368; -.
DR   eggNOG; arCOG01748; Archaea.
DR   HOGENOM; CLU_027272_2_0_2; -.
DR   OMA; KKNPDVF; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000001431; 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   Gene3D; 1.10.275.10; -; 1.
DR   HAMAP; MF_00006; Arg_succ_lyase; 1.
DR   InterPro; IPR009049; Argininosuccinate_lyase.
DR   InterPro; IPR024083; Fumarase/histidase_N.
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; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; SSF48557; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Lyase.
FT   CHAIN           1..429
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000089105"
SQ   SEQUENCE   429 AA;  46725 MW;  FDB87D6D3F15F258 CRC64;
     MAFYRSWIGG GGDLVRRYTS SMADDVEIAE EVVKILKTHV AHLAEVGVIP REAAERIAKA
     LDEVDYDALA KGGFEDIHEA VEKWVIDRVG EEAGGWLGLG RSRNDHVAAA IRLAALRKLA
     ELKRGLAALR CALAKRALQY ADCAMPSFTH FQPAQAITFG HYLLSIDELV EEFSRALAGV
     EPLLKRSPLG AGPAGGVKTP IDRRRLAKAL GFEDVVGNAL YASGSRFFAS AAASIVVSFL
     VELSRYVDDF IRWNSPAIGY VKAPDSHVST SSIMPHKRNL VTLEVLRARI SEAVGHLTAL
     YAVQAKIGAG YSLDLQEATR HLWAILKIAG EGVEVLRDFV EGLEFNCEKA RLDAETYYAT
     SSDTAEAIAL SGVPFRRAYF QLAEEIKRGS AKLLSPEEAV KRPTEGSANP EEVRRAASAR
     LIFCKTPAF
 
 
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