CPKA_PYRFU
ID CPKA_PYRFU Reviewed; 314 AA.
AC P95474;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Carbamate kinase;
DE EC=2.7.2.2;
DE AltName: Full=Carbamate kinase-like carbamoylphosphate synthase;
GN Name=cpkA; Synonyms=cpa; OrderedLocusNames=PF0676;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=9371756; DOI=10.1073/pnas.94.24.12803;
RA Durbecq V., Legrain C., Roovers M., Pierard A., Glansdorff N.;
RT "The carbamate kinase-like carbamoyl phosphate synthetase of the
RT hyperthermophilic archaeon Pyrococcus furiosus, a missing link in the
RT evolution of carbamoyl phosphate biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:12803-12808(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RA Kanai A., Oida H., Yabe T., Hihara S., Doi H.;
RT "Pfu helicase locus.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), AND FUNCTION.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10860751; DOI=10.1006/jmbi.2000.3779;
RA Ramon-Maiques S., Marina A., Uriarte M., Fita I., Rubio V.;
RT "The 1.5-A resolution crystal structure of the carbamate kinase-like
RT carbamoyl phosphate synthetase from the hyperthermophilic Archaeon
RT Pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme
RT is a carbamate kinase, and provides insight into substrate binding and
RT stability in carbamate kinases.";
RL J. Mol. Biol. 299:463-476(2000).
CC -!- FUNCTION: Carbamate kinase that plays a biosynthetic role in that it
CC produces carbamoyl-phosphate. {ECO:0000269|PubMed:10860751}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC 50% activity is retained after 1 hour at 100 degrees Celsius or 3
CC hours at 95 degrees Celsius.;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the carbamate kinase family. {ECO:0000305}.
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DR EMBL; Y09829; CAA70972.1; -; Genomic_DNA.
DR EMBL; AB016521; BAA32017.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL80800.1; -; Genomic_DNA.
DR PIR; T43855; T43855.
DR RefSeq; WP_011011798.1; NC_018092.1.
DR PDB; 1E19; X-ray; 1.50 A; A/B=1-314.
DR PDBsum; 1E19; -.
DR AlphaFoldDB; P95474; -.
DR SMR; P95474; -.
DR STRING; 186497.PF0676; -.
DR EnsemblBacteria; AAL80800; AAL80800; PF0676.
DR GeneID; 41712479; -.
DR KEGG; pfu:PF0676; -.
DR PATRIC; fig|186497.12.peg.712; -.
DR eggNOG; arCOG00863; Archaea.
DR HOGENOM; CLU_076278_0_0_2; -.
DR OMA; QPMDVAG; -.
DR OrthoDB; 77437at2157; -.
DR PhylomeDB; P95474; -.
DR BRENDA; 2.7.2.2; 5243.
DR EvolutionaryTrace; P95474; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008804; F:carbamate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006525; P:arginine metabolic process; IEA:InterPro.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..314
FT /note="Carbamate kinase"
FT /id="PRO_0000185149"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:1E19"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:1E19"
FT HELIX 23..42
FT /evidence="ECO:0007829|PDB:1E19"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:1E19"
FT HELIX 54..71
FT /evidence="ECO:0007829|PDB:1E19"
FT HELIX 78..103
FT /evidence="ECO:0007829|PDB:1E19"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1E19"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1E19"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1E19"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:1E19"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:1E19"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:1E19"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:1E19"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:1E19"
FT HELIX 176..184
FT /evidence="ECO:0007829|PDB:1E19"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1E19"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:1E19"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:1E19"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:1E19"
FT HELIX 215..225
FT /evidence="ECO:0007829|PDB:1E19"
FT STRAND 229..239
FT /evidence="ECO:0007829|PDB:1E19"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:1E19"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:1E19"
FT HELIX 257..265
FT /evidence="ECO:0007829|PDB:1E19"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:1E19"
FT HELIX 274..287
FT /evidence="ECO:0007829|PDB:1E19"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:1E19"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:1E19"
FT HELIX 300..304
FT /evidence="ECO:0007829|PDB:1E19"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:1E19"
SQ SEQUENCE 314 AA; 34429 MW; B4496B827581EF42 CRC64;
MGKRVVIALG GNALQQRGQK GSYEEMMDNV RKTARQIAEI IARGYEVVIT HGNGPQVGSL
LLHMDAGQAT YGIPAQPMDV AGAMSQGWIG YMIQQALKNE LRKRGMEKKV VTIITQTIVD
KNDPAFQNPT KPVGPFYDEE TAKRLAREKG WIVKEDSGRG WRRVVPSPDP KGHVEAETIK
KLVERGVIVI ASGGGGVPVI LEDGEIKGVE AVIDKDLAGE KLAEEVNADI FMILTDVNGA
ALYYGTEKEQ WLREVKVEEL RKYYEEGHFK AGSMGPKVLA AIRFIEWGGE RAIIAHLEKA
VEALEGKTGT QVLP
