位置:首页 > 蛋白库 > ARLY_BRUSU
ARLY_BRUSU
ID   ARLY_BRUSU              Reviewed;         466 AA.
AC   Q8FYA4; G0K8K1;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 111.
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=BR1981, BS1330_I1975;
OS   Brucella suis biovar 1 (strain 1330).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=204722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA   Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA   Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between animal
RT   and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=22038969; DOI=10.1128/jb.06181-11;
RA   Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT   "Revised genome sequence of Brucella suis 1330.";
RL   J. Bacteriol. 193:6410-6410(2011).
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}.
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; AE014291; AAN30871.1; -; Genomic_DNA.
DR   EMBL; CP002997; AEM19288.1; -; Genomic_DNA.
DR   RefSeq; WP_004687711.1; NZ_KN046804.1.
DR   AlphaFoldDB; Q8FYA4; -.
DR   SMR; Q8FYA4; -.
DR   EnsemblBacteria; AEM19288; AEM19288; BS1330_I1975.
DR   GeneID; 45125245; -.
DR   GeneID; 55591562; -.
DR   KEGG; bms:BR1981; -.
DR   KEGG; bsi:BS1330_I1975; -.
DR   PATRIC; fig|204722.22.peg.2031; -.
DR   HOGENOM; CLU_027272_2_3_5; -.
DR   OMA; KKNPDVF; -.
DR   PhylomeDB; Q8FYA4; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000007104; Chromosome I.
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.
FT   CHAIN           1..466
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_0000137747"
SQ   SEQUENCE   466 AA;  51285 MW;  CE957213BDE31D32 CRC64;
     MSEQKSSNQM WGGRFASGPD AIMEEINASI GFDRKLYAQD IQGSLAHAAM LAKTGIIAAE
     DHKQIENGLK TIRKEIEEGK FTFSRKLEDI HMNIEARLAE LIGPAAGRLH TARSRNDQVA
     VDFRLWVKQE LEKTAAALKN LIEAFLERAE EHAATVMPGF THLQTAQPVT FGHHCMAYVE
     MFGRDLSRVR DAIERMDESP LGAAALAGTG FPIDRHMTAK ALGFREPTRN SLDSVSDRDY
     ALEFLSLAAI CAGHLSRLAE EIVIWSTPQF NFVRLSDAFS TGSSIMPQKK NPDAAELVRA
     KTGRINGSLV ALLTIMKGLP LAYSKDMQED KEQVFDAAEN LELAIAAMAG MVRDLTVNVA
     AMKKAAGSGY STATDLADWL VRTLGLPFRE AHHVTGRAVA LAESRKVDLA KLSLEELQSI
     NPAITAEVFG YLTVEKSVKS RQSFGGTAPQ EVRRQIRYWK KRIAKA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024