NAGH_RALSP
ID NAGH_RALSP Reviewed; 161 AA.
AC O52380;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Salicylate 5-hydroxylase, small oxygenase component;
DE Short=S5H small oxygenase component;
DE EC=1.14.13.172;
DE AltName: Full=Salicylate 5-hydroxylase, oxygenase component NagH;
DE AltName: Full=Salicylate 5-monooxygenase, hydroxylase small subunit;
GN Name=nagH {ECO:0000312|EMBL:AAD12608.1};
OS Ralstonia sp.
OG Plasmid pWWU2 {ECO:0000312|EMBL:AAD12608.1}.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=54061;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAD12608.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, DISRUPTION PHENOTYPE,
RP AND SUBUNIT.
RC STRAIN=U2 {ECO:0000312|EMBL:AAD12608.1};
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] {ECO:0000303|PubMed:11872705}
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, PATHWAY, AND SUBUNIT.
RC STRAIN=U2 {ECO:0000269|PubMed:11872705};
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: Oxygenase component of the salicylate 5-hydroxylase (S5H)
CC multicomponent enzyme system which catalyzes the 5-hydroxylation of
CC salicylate to gentisate. Active only on substrates with a ring-
CC substituted carboxylate group with an adjacent hydroxyl group.
CC Primarily active against salicylate and substituted salicylates, but
CC not against 2-hydroxycinnamate, 3-hydroxycinnamate, 2-
CC hydroxyphenylacetate, 3-hydroxyphenylacetate, 2-hydroxybenzophenone, 1-
CC hydroxy-2-naphthoate, 4-methoxysalicylate or 2-hydroxyacetophenone.
CC {ECO:0000269|PubMed:11872705, ECO:0000269|PubMed:9573207}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + O2 + salicylate = 2,5-dihydroxybenzoate + H2O +
CC NAD(+); Xref=Rhea:RHEA:35307, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:30762, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58044; EC=1.14.13.172;
CC Evidence={ECO:0000269|PubMed:11872705};
CC -!- PATHWAY: Aromatic compound metabolism; naphthalene degradation.
CC {ECO:0000269|PubMed:11872705, ECO:0000269|PubMed:9573207}.
CC -!- SUBUNIT: The salicylate 5-hydroxylase (S5H) multicomponent enzyme
CC system is composed of an electron transfer component and an oxygenase
CC component. The electron transfer component is comprised of a ferredoxin
CC reductase (NagAa) and a ferredoxin (NagAb), and the oxygenase component
CC is formed by a large subunit (NagG) and a small subunit (NagH).
CC {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 beta subunit family. {ECO:0000305}.
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DR EMBL; AF036940; AAD12608.1; -; Genomic_DNA.
DR PDB; 7C8Z; X-ray; 2.60 A; B/D/F/H=1-161.
DR PDBsum; 7C8Z; -.
DR AlphaFoldDB; O52380; -.
DR SMR; O52380; -.
DR KEGG; ag:AAD12608; -.
DR BioCyc; MetaCyc:MON-14767; -.
DR BRENDA; 1.14.13.172; 5085.
DR UniPathway; UPA00082; -.
DR GO; GO:1902494; C:catalytic complex; IDA:UniProtKB.
DR GO; GO:0034785; F:salicylate 5-hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046244; P:salicylic acid catabolic process; IGI:UniProtKB.
DR CDD; cd00667; ring_hydroxylating_dioxygenases_beta; 1.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR000391; Rng_hydr_dOase-bsu.
DR InterPro; IPR037401; SnoaL-like.
DR Pfam; PF13577; SnoaL_4; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Monooxygenase; NAD;
KW Oxidoreductase; Plasmid.
FT CHAIN 1..161
FT /note="Salicylate 5-hydroxylase, small oxygenase component"
FT /id="PRO_0000421810"
FT HELIX 4..20
FT /evidence="ECO:0007829|PDB:7C8Z"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 33..43
FT /evidence="ECO:0007829|PDB:7C8Z"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:7C8Z"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 100..115
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 120..135
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 138..149
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:7C8Z"
SQ SEQUENCE 161 AA; 18813 MW; 38E7B36F281A9A01 CRC64;
MVDFKTYFEL LNLYSDYAMV CDSANWEKWP DFFIETGTYR LQPRENFEQG LPLCLLALES
KAMIRDRVYG VKETMYHDPY YQRHIVGTPR VLSVERDADG ERITAEASYA VIRTKYDGDS
TIFNAGYYRD VIVRTPEGLK LKSRLCVYDS EMIPNSVIYP I
