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ARLY_SYNP6
ID   ARLY_SYNP6              Reviewed;         466 AA.
AC   Q5N1K1;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 104.
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=syc1629_c;
OS   Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS   nidulans).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=269084;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX   PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA   Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA   Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT   "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT   Synechococcus elongatus PCC 6301 chromosome: gene content and
RT   organization.";
RL   Photosyn. Res. 93:55-67(2007).
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; AP008231; BAD79819.1; -; Genomic_DNA.
DR   RefSeq; WP_011243939.1; NC_006576.1.
DR   AlphaFoldDB; Q5N1K1; -.
DR   SMR; Q5N1K1; -.
DR   STRING; 269084.syc1629_c; -.
DR   EnsemblBacteria; BAD79819; BAD79819; syc1629_c.
DR   KEGG; syc:syc1629_c; -.
DR   eggNOG; COG0165; Bacteria.
DR   OMA; KKNPDVF; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000001175; 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; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Lyase.
FT   CHAIN           1..466
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_0000137838"
SQ   SEQUENCE   466 AA;  51822 MW;  9B41900A8F2BC851 CRC64;
     MTQAAAPQPW SDRFETALHP AIVVFNASIG FDLALIEYDL TGSQAHAQML AEQDIISREE
     GEAIVAGLEQ IRSEYRTGQF QPGLDAEDVH FAVERRLTEL LGDVGKKLHT ARSRNDQVGT
     DTRLYLRDRV DHIRQQLRDY QRVLLSQAEQ HLETLIPGYT HLQRAQPLSL AHHLHAYLEM
     AERDWERLGD LRKRLNTSPL GAGALAGTTF PIDRQRTAAL LGFERIYANS LDAVSDRDSL
     VEFLAAASLI MVHLSRLAEE VILWASEEFR FVRLSDRCAT GSSITPQKKN PDVPELVRGK
     TGRVFGHLQA LLVVLKGLPL AYNKDLQEDK EGLFDAVQTV ESCLEAMTIL FAEGLSFQPD
     RLAAAVEADF SNATDVADYL AARGVPFREA YNLVGRVVRT CLEQGKLLKD LSLAEWQALH
     PQFEADIYTA IAPQQVVAAR NSLGGTGFEQ VRSALASVRQ RLEATC
 
 
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