NAGG_RALSP
ID NAGG_RALSP Reviewed; 423 AA.
AC O52379;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Salicylate 5-hydroxylase, large oxygenase component;
DE Short=S5H large oxygenase component;
DE EC=1.14.13.172;
DE AltName: Full=Salicylate 5-hydroxylase, oxygenase component NagG;
DE AltName: Full=Salicylate 5-monooxygenase, hydroxylase large subunit;
GN Name=nagG {ECO:0000312|EMBL:AAD12607.1};
OS Ralstonia sp.
OG Plasmid pWWU2 {ECO:0000312|EMBL:AAD12607.1}.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=54061;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAD12607.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, DISRUPTION PHENOTYPE,
RP AND SUBUNIT.
RC STRAIN=U2 {ECO:0000312|EMBL:AAD12607.1};
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:0000305}
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 -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00628};
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 alpha subunit family. {ECO:0000305}.
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DR EMBL; AF036940; AAD12607.1; -; Genomic_DNA.
DR PDB; 7C8Z; X-ray; 2.60 A; A/C/E/G=1-423.
DR PDBsum; 7C8Z; -.
DR AlphaFoldDB; O52379; -.
DR SMR; O52379; -.
DR PRIDE; O52379; -.
DR KEGG; ag:AAD12607; -.
DR BioCyc; MetaCyc:MON-14766; -.
DR BRENDA; 1.14.13.172; 5085.
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:0005506; F:iron ion binding; IEA:InterPro.
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; cd08880; RHO_alpha_C_ahdA1c-like; 1.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR043264; AhdA1c-like_alpha_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756; PTHR43756; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Aromatic hydrocarbons catabolism; Iron; Iron-sulfur;
KW Metal-binding; Monooxygenase; NAD; Oxidoreductase; Plasmid.
FT CHAIN 1..423
FT /note="Salicylate 5-hydroxylase, large oxygenase component"
FT /id="PRO_0000421808"
FT DOMAIN 49..168
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 91
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:O85673,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 93
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:O85673,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 111
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:O85673,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 114
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:O85673,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 224
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O85673"
FT BINDING 229
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O85673"
FT BINDING 370
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O85673"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:7C8Z"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:7C8Z"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:7C8Z"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:7C8Z"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:7C8Z"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:7C8Z"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:7C8Z"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:7C8Z"
FT HELIX 177..192
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 198..208
FT /evidence="ECO:0007829|PDB:7C8Z"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:7C8Z"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:7C8Z"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 301..307
FT /evidence="ECO:0007829|PDB:7C8Z"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 319..327
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 333..342
FT /evidence="ECO:0007829|PDB:7C8Z"
FT HELIX 347..356
FT /evidence="ECO:0007829|PDB:7C8Z"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:7C8Z"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:7C8Z"
FT HELIX 368..383
FT /evidence="ECO:0007829|PDB:7C8Z"
FT TURN 393..396
FT /evidence="ECO:0007829|PDB:7C8Z"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:7C8Z"
FT HELIX 408..421
FT /evidence="ECO:0007829|PDB:7C8Z"
SQ SEQUENCE 423 AA; 48795 MW; 2EDC17B117974DC2 CRC64;
MSEPQRLKPV FPQDPKWPGE GSSRVPFWAY TREDLYKREL ERLFYANHWC YVGLEAEIPN
PGDFKRTVIG ERSVIMVRDP DGGINVVENV CAHRGMRFCR ERHGNAKDFF CPYHQWNYSL
KGDLQGVPFR RGVKQDGKVN GGMPKDFKLE EHGLTKLKVA ARGGAVFASF DHDVEPFEEF
LGPTILHYFD RVFNGRKLKI LGYRRQRIPG NWKLMQENIK DPYHPGLLHT WFSTFGLWRA
DNKSELKMDA KFRHAAMIST RGQGGKNEEV VSGVDSFKEQ MKVNDPRLLD IVPEPWWGGP
TAVMTTIFPS VIIQQQVNSV STRHIQPNGH GSFDFVWTHF GFEDDNEEWT QRRLIQANLF
GPAGFVSADD GEVIEWSQEG FEQKPTHRTV IEMGGHEIGD TDHMVTETLI RGMYDYWRKV
MGE
