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ARCC_ECOLI
ID   ARCC_ECOLI              Reviewed;         297 AA.
AC   P37306; P77419; Q2MBQ8;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Carbamate kinase;
DE            EC=2.7.2.2;
GN   Name=arcC; Synonyms=ybcF; OrderedLocusNames=b0521, JW0510;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 203-297.
RX   PubMed=2644189; DOI=10.1128/jb.171.1.198-204.1989;
RA   Watanabe W., Sampei G., Aiba A., Mizobuchi K.;
RT   "Identification and sequence analysis of Escherichia coli purE and purK
RT   genes encoding 5'-phosphoribosyl-5-amino-4-imidazole carboxylase for de
RT   novo purine biosynthesis.";
RL   J. Bacteriol. 171:198-204(1989).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 203-297.
RC   STRAIN=K12;
RX   PubMed=2464576; DOI=10.1128/jb.171.1.205-212.1989;
RA   Tiedeman A.A., Keyhani J., Kamholz J., Daum H.A. III, Gots J.S.,
RA   Smith J.M.;
RT   "Nucleotide sequence analysis of the purEK operon encoding 5'-
RT   phosphoribosyl-5-aminoimidazole carboxylase of Escherichia coli K-12.";
RL   J. Bacteriol. 171:205-212(1989).
RN   [6]
RP   IDENTIFICATION.
RX   PubMed=7940673; DOI=10.1016/0968-0004(94)90067-1;
RA   Borodovsky M., Koonin E.V., Rudd K.E.;
RT   "New genes in old sequence: a strategy for finding genes in the bacterial
RT   genome.";
RL   Trends Biochem. Sci. 19:309-313(1994).
RN   [7]
RP   IDENTIFICATION.
RX   PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA   Borodovsky M., Rudd K.E., Koonin E.V.;
RT   "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT   genome.";
RL   Nucleic Acids Res. 22:4756-4767(1994).
RN   [8]
RP   IDENTIFICATION.
RX   PubMed=7920643; DOI=10.1038/ng0694-205;
RA   Robison K., Gilbert W., Church G.M.;
RT   "Large scale bacterial gene discovery by similarity search.";
RL   Nat. Genet. 7:205-214(1994).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + NH4(+) = ADP + carbamoyl phosphate +
CC         H(+) + H2O; Xref=Rhea:RHEA:10152, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58228, ChEBI:CHEBI:456216; EC=2.7.2.2;
CC   -!- PATHWAY: Metabolic intermediate metabolism; carbamoyl phosphate
CC       degradation; CO(2) and NH(3) from carbamoyl phosphate: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the carbamate kinase family. {ECO:0000305}.
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DR   EMBL; U82664; AAB40273.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73623.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76298.1; -; Genomic_DNA.
DR   EMBL; M19657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X12982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; H64783; H64783.
DR   RefSeq; NP_415054.1; NC_000913.3.
DR   RefSeq; WP_000855379.1; NZ_LN832404.1.
DR   AlphaFoldDB; P37306; -.
DR   SMR; P37306; -.
DR   BioGRID; 4262013; 3.
DR   IntAct; P37306; 3.
DR   STRING; 511145.b0521; -.
DR   PaxDb; P37306; -.
DR   PRIDE; P37306; -.
DR   EnsemblBacteria; AAC73623; AAC73623; b0521.
DR   EnsemblBacteria; BAE76298; BAE76298; BAE76298.
DR   GeneID; 944972; -.
DR   KEGG; ecj:JW0510; -.
DR   KEGG; eco:b0521; -.
DR   PATRIC; fig|1411691.4.peg.1757; -.
DR   EchoBASE; EB2285; -.
DR   eggNOG; COG0549; Bacteria.
DR   HOGENOM; CLU_076278_0_1_6; -.
DR   InParanoid; P37306; -.
DR   OMA; ESQGFIG; -.
DR   PhylomeDB; P37306; -.
DR   BioCyc; EcoCyc:EG12384-MON; -.
DR   SABIO-RK; P37306; -.
DR   UniPathway; UPA00996; UER00366.
DR   PRO; PR:P37306; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008804; F:carbamate kinase activity; IBA:GO_Central.
DR   GO; GO:0019546; P:arginine deiminase pathway; IBA:GO_Central.
DR   GO; GO:0035975; P:carbamoyl phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd04235; AAK_CK; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR003964; Carb_kinase.
DR   PANTHER; PTHR30409; PTHR30409; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   PIRSF; PIRSF000723; Carbamate_kin; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   TIGRFAMs; TIGR00746; arcC; 1.
PE   3: Inferred from homology;
KW   Arginine metabolism; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..297
FT                   /note="Carbamate kinase"
FT                   /id="PRO_0000185119"
FT   CONFLICT        279..297
FT                   /note="ALSRIEETLAGEAGTCISL -> RYRELKRRWRAKRGPVFRCSRRH (in
FT                   Ref. 5; X12982)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   297 AA;  31644 MW;  0169371E119AE832 CRC64;
     MKTLVVALGG NALLQRGEAL TAENQYRNIA SAVPALARLA RSYRLAIVHG NGPQVGLLAL
     QNLAWKEVEP YPLDVLVAES QGMIGYMLAQ SLSAQPQMPP VTTVLTRIEV SPDDPAFLQP
     EKFIGPVYQP EEQEALEAAY GWQMKRDGKY LRRVVASPQP RKILDSEAIE LLLKEGHVVI
     CSGGGGVPVT DDGAGSEAVI DKDLAAALLA EQINADGLVI LTDADAVYEN WGTPQQRAIR
     HATPDELAPF AKADGSMGPN VTAVSGYVRS RGKPAWIGAL SRIEETLAGE AGTCISL
 
 
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