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NAGAB_RALSP
ID   NAGAB_RALSP             Reviewed;         104 AA.
AC   O52381;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Naphthalene 1,2-dioxygenase/salicylate 5-hydroxylase systems, ferredoxin component {ECO:0000303|PubMed:11872705};
DE            Short=NDO/S5H systems ferredoxin component {ECO:0000303|PubMed:11872705};
DE   AltName: Full=Ferredoxin NagAb {ECO:0000303|PubMed:9573207};
GN   Name=nagAb {ECO:0000303|PubMed:9573207};
OS   Ralstonia sp.
OG   Plasmid pWWU2 {ECO:0000312|EMBL:AAD12609.1}.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=54061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, DISRUPTION PHENOTYPE,
RP   AND SUBUNIT.
RC   STRAIN=U2 {ECO:0000312|EMBL:AAD12609.1};
RX   PubMed=9573207; DOI=10.1128/jb.180.9.2522-2530.1998;
RA   Fuenmayor S.L., Wild M., Boyes A.L., Williams P.A.;
RT   "A gene cluster encoding steps in conversion of naphthalene to gentisate in
RT   Pseudomonas sp. strain U2.";
RL   J. Bacteriol. 180:2522-2530(1998).
RN   [2]
RP   FUNCTION, PATHWAY, AND SUBUNIT.
RC   STRAIN=U2;
RX   PubMed=11872705; DOI=10.1128/jb.184.6.1547-1555.2002;
RA   Zhou N.Y., Al-Dulayymi J., Baird M.S., Williams P.A.;
RT   "Salicylate 5-hydroxylase from Ralstonia sp. strain U2: a monooxygenase
RT   with close relationships to and shared electron transport proteins with
RT   naphthalene dioxygenase.";
RL   J. Bacteriol. 184:1547-1555(2002).
CC   -!- FUNCTION: Component of two multicomponent enzyme systems which are
CC       involved in the catabolism of naphthalene (PubMed:11872705,
CC       PubMed:9573207). Plays a role as an electron transfer component for
CC       both salicylate 5-hydroxylase (S5H) and naphthalene 1,2-dioxygenase
CC       (NDO) systems, by transferring electrons to the oxygenase components
CC       (PubMed:11872705, PubMed:9573207). {ECO:0000269|PubMed:11872705,
CC       ECO:0000269|PubMed:9573207}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000250|UniProtKB:P0A185,
CC         ECO:0000255|PROSITE-ProRule:PRU00628};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit.
CC       {ECO:0000250|UniProtKB:P0A185, ECO:0000255|PROSITE-ProRule:PRU00628};
CC   -!- PATHWAY: Aromatic compound metabolism; naphthalene degradation.
CC       {ECO:0000269|PubMed:11872705, ECO:0000269|PubMed:9573207}.
CC   -!- SUBUNIT: Ferredoxin NagAb belongs to both the salicylate 5-hydroxylase
CC       (S5H) and the naphthalene 1,2-dioxygenase (NDO) multicomponent enzyme
CC       systems. The NDO multicomponent enzyme system is composed of an
CC       electron transfer component and a dioxygenase component (iron sulfur
CC       protein (ISP)). The electron transfer component is composed of a
CC       ferredoxin reductase (NagAa) and a ferredoxin (NagAb), and the
CC       dioxygenase component is formed by a large alpha subunit (NagAc) and a
CC       small beta subunit (NagAd). The S5H multicomponent enzyme system is
CC       composed of an electron transfer component and a monooxygenase
CC       component. The electron transfer component is composed of a ferredoxin
CC       reductase (NagAa) and a ferredoxin (NagAb), and the monooxygenase
CC       component is formed by a large subunit (NagG) and a small subunit
CC       (NagH). {ECO:0000269|PubMed:11872705, ECO:0000269|PubMed:9573207}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are not able to convert
CC       salicylate to gentisate. {ECO:0000269|PubMed:9573207}.
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC       ferredoxin component family. {ECO:0000305}.
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DR   EMBL; AF036940; AAD12609.1; -; Genomic_DNA.
DR   AlphaFoldDB; O52381; -.
DR   SMR; O52381; -.
DR   UniPathway; UPA00082; -.
DR   GO; GO:1902494; C:catalytic complex; IDA:UniProtKB.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0022900; P:electron transport chain; IDA:UniProtKB.
DR   GO; GO:1901170; P:naphthalene catabolic process; IDA:UniProtKB.
DR   GO; GO:0046244; P:salicylic acid catabolic process; IDA:UniProtKB.
DR   Gene3D; 2.102.10.10; -; 1.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   Pfam; PF00355; Rieske; 1.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; Aromatic hydrocarbons catabolism; Electron transport; Iron;
KW   Iron-sulfur; Metal-binding; Plasmid; Transport.
FT   CHAIN           1..104
FT                   /note="Naphthalene 1,2-dioxygenase/salicylate 5-hydroxylase
FT                   systems, ferredoxin component"
FT                   /id="PRO_0000421807"
FT   DOMAIN          6..101
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         45
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:P0A185,
FT                   ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         47
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:P0A185,
FT                   ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         64
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:P0A185,
FT                   ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         67
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:P0A185,
FT                   ECO:0000255|PROSITE-ProRule:PRU00628"
SQ   SEQUENCE   104 AA;  11565 MW;  BF761247B7579FF8 CRC64;
     MTQNWIDAAC LDDIPEGDVV GVKVNGKEIA LYEVEGEIYA TDNLCTHGAA RMSDGFLEGR
     EIECPLHQGR FDVCTGKALC TPLTKDIKTY PVKIENMRVM LKME
 
 
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