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COAE_HAEIN
ID   COAE_HAEIN              Reviewed;         206 AA.
AC   P44920;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Dephospho-CoA kinase {ECO:0000255|HAMAP-Rule:MF_00376};
DE            EC=2.7.1.24 {ECO:0000255|HAMAP-Rule:MF_00376};
DE   AltName: Full=Dephosphocoenzyme A kinase {ECO:0000255|HAMAP-Rule:MF_00376};
GN   Name=coaE {ECO:0000255|HAMAP-Rule:MF_00376}; OrderedLocusNames=HI_0890;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of
CC       dephosphocoenzyme A to form coenzyme A. {ECO:0000255|HAMAP-
CC       Rule:MF_00376}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-dephospho-CoA + ATP = ADP + CoA + H(+);
CC         Xref=Rhea:RHEA:18245, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216;
CC         EC=2.7.1.24; Evidence={ECO:0000255|HAMAP-Rule:MF_00376};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC       pantothenate: step 5/5. {ECO:0000255|HAMAP-Rule:MF_00376}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00376}.
CC   -!- SIMILARITY: Belongs to the CoaE family. {ECO:0000255|HAMAP-
CC       Rule:MF_00376, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC22550.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L42023; AAC22550.1; ALT_INIT; Genomic_DNA.
DR   PIR; A64161; A64161.
DR   RefSeq; NP_439051.1; NC_000907.1.
DR   RefSeq; WP_010869082.1; NC_000907.1.
DR   PDB; 1JJV; X-ray; 2.00 A; A=1-206.
DR   PDBsum; 1JJV; -.
DR   AlphaFoldDB; P44920; -.
DR   SMR; P44920; -.
DR   STRING; 71421.HI_0890; -.
DR   EnsemblBacteria; AAC22550; AAC22550; HI_0890.
DR   KEGG; hin:HI_0890; -.
DR   PATRIC; fig|71421.8.peg.932; -.
DR   eggNOG; COG0237; Bacteria.
DR   HOGENOM; CLU_057180_1_2_6; -.
DR   PhylomeDB; P44920; -.
DR   BioCyc; HINF71421:G1GJ1-930-MON; -.
DR   BRENDA; 2.7.1.24; 2529.
DR   UniPathway; UPA00241; UER00356.
DR   EvolutionaryTrace; P44920; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004140; F:dephospho-CoA kinase activity; IBA:GO_Central.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00376; Dephospho_CoA_kinase; 1.
DR   InterPro; IPR001977; Depp_CoAkinase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01121; CoaE; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00152; TIGR00152; 1.
DR   PROSITE; PS51219; DPCK; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..206
FT                   /note="Dephospho-CoA kinase"
FT                   /id="PRO_0000172947"
FT   DOMAIN          4..204
FT                   /note="DPCK"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT   BINDING         12..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:1JJV"
FT   HELIX           15..23
FT                   /evidence="ECO:0007829|PDB:1JJV"
FT   TURN            24..26
FT                   /evidence="ECO:0007829|PDB:1JJV"
FT   STRAND          29..31
FT                   /evidence="ECO:0007829|PDB:1JJV"
FT   HELIX           32..38
FT                   /evidence="ECO:0007829|PDB:1JJV"
FT   HELIX           45..54
FT                   /evidence="ECO:0007829|PDB:1JJV"
FT   HELIX           67..75
FT                   /evidence="ECO:0007829|PDB:1JJV"
FT   HELIX           78..101
FT                   /evidence="ECO:0007829|PDB:1JJV"
FT   STRAND          105..111
FT                   /evidence="ECO:0007829|PDB:1JJV"
FT   TURN            113..119
FT                   /evidence="ECO:0007829|PDB:1JJV"
FT   HELIX           121..123
FT                   /evidence="ECO:0007829|PDB:1JJV"
FT   STRAND          125..131
FT                   /evidence="ECO:0007829|PDB:1JJV"
FT   HELIX           134..141
FT                   /evidence="ECO:0007829|PDB:1JJV"
FT   HELIX           149..158
FT                   /evidence="ECO:0007829|PDB:1JJV"
FT   HELIX           162..168
FT                   /evidence="ECO:0007829|PDB:1JJV"
FT   STRAND          170..174
FT                   /evidence="ECO:0007829|PDB:1JJV"
FT   HELIX           179..203
FT                   /evidence="ECO:0007829|PDB:1JJV"
SQ   SEQUENCE   206 AA;  23287 MW;  DF85B65D50131C01 CRC64;
     MTYIVGLTGG IGSGKTTIAN LFTDLGVPLV DADVVAREVV AKDSPLLSKI VEHFGAQILT
     EQGELNRAAL RERVFNHDED KLWLNNLLHP AIRERMKQKL AEQTAPYTLF VVPLLIENKL
     TALCDRILVV DVSPQTQLAR SAQRDNNNFE QIQRIMNSQV SQQERLKWAD DVINNDAELA
     QNLPHLQQKV LELHQFYLQQ AENKNA
 
 
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