3HBH_CORGL
ID 3HBH_CORGL Reviewed; 442 AA.
AC Q8NLB6; Q6M1I4;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=3-hydroxybenzoate 6-hydroxylase;
DE EC=1.14.13.24;
GN OrderedLocusNames=Cgl3026, cg3354;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [3]
RP FUNCTION IN 3-HYDROXYBENZOATE ASSIMILATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=16000747; DOI=10.1128/aem.71.7.3442-3452.2005;
RA Shen X.H., Jiang C.Y., Huang Y., Liu Z.P., Liu S.J.;
RT "Functional identification of novel genes involved in the glutathione-
RT independent gentisate pathway in Corynebacterium glutamicum.";
RL Appl. Environ. Microbiol. 71:3442-3452(2005).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBSTRATE
RP SPECIFICITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=20806251; DOI=10.1002/jobm.201000053;
RA Yang Y.F., Zhang J.J., Wang S.H., Zhou N.Y.;
RT "Purification and characterization of the ncgl2923-encoded 3-
RT hydroxybenzoate 6-hydroxylase from Corynebacterium glutamicum.";
RL J. Basic Microbiol. 50:599-604(2010).
CC -!- FUNCTION: Catalyzes the NADH-dependent conversion of 3-hydroxybenzoate
CC to gentisate (2,5-dihydroxybenzoate). Is involved in the utilization of
CC 3-hydroxybenzoate as a sole source of carbon and energy for
CC C.glutamicum growth. Displays a high preference for NADH over NADPH as
CC cosubstrate. Is not active with 4-hydroxybenzoate, salicylate,
CC protocatechuate or benzoate as substrates.
CC {ECO:0000269|PubMed:16000747, ECO:0000269|PubMed:20806251}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxybenzoate + H(+) + NADH + O2 = 2,5-dihydroxybenzoate +
CC H2O + NAD(+); Xref=Rhea:RHEA:22692, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16193,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58044;
CC EC=1.14.13.24; Evidence={ECO:0000269|PubMed:20806251};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:20806251};
CC -!- ACTIVITY REGULATION: Activity is reduced by the addition of 0.1 mM of
CC various metal ions, including Ca(2+) (16%), Mn(2+) (20%), K(+) (30%),
CC Zn(2+) (64%) and Cu(2+) (83%). However, the addition of 0.1 mM Mg(2+)
CC enhances activity by 16%. {ECO:0000269|PubMed:20806251}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=53.4 uM for 3-hydroxybenzoate {ECO:0000269|PubMed:20806251};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:20806251};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:20806251}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show an altered growth
CC with 3-hydroxybenzoate as sole source, but growth with gentisate and
CC other aromatic substrates (benzoate, 4-hydroxybenzoate, and
CC protocatechuate) is the same as that of wild-type.
CC {ECO:0000269|PubMed:16000747}.
CC -!- SIMILARITY: Belongs to the 3-hydroxybenzoate 6-hydroxylase family.
CC {ECO:0000305}.
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DR EMBL; BA000036; BAC00420.1; -; Genomic_DNA.
DR EMBL; BX927157; CAF18966.1; -; Genomic_DNA.
DR RefSeq; NP_602220.1; NC_003450.3.
DR RefSeq; WP_011015578.1; NC_006958.1.
DR AlphaFoldDB; Q8NLB6; -.
DR SMR; Q8NLB6; -.
DR STRING; 196627.cg3354; -.
DR KEGG; cgb:cg3354; -.
DR KEGG; cgl:Cgl3026; -.
DR PATRIC; fig|196627.13.peg.2961; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_009665_19_3_11; -.
DR OMA; KDWDPRI; -.
DR BRENDA; 1.14.13.24; 960.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0018669; F:3-hydroxybenzoate 6-monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0019439; P:aromatic compound catabolic process; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; FAD; Flavoprotein; Monooxygenase; NAD;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..442
FT /note="3-hydroxybenzoate 6-hydroxylase"
FT /id="PRO_0000413330"
SQ SEQUENCE 442 AA; 49648 MW; FC3BE4010455A2B6 CRC64;
MSLPHSDELR GQKIIISGGG IGGAAGALAL ALRGADVTLY ERAAEFKEVG AGLQIGPHGW
RMLESWGLLD QIVVAGYLPE DMQFRDAVNR ETILTMRFDE EFQQHYGGRY LVIHRSDLLN
ILVTNAEAAG AKLHNGVLVT DSRTVDGGIE VDIESSINKG EDNKTLLVDA FLAFDGIHSV
MRKKLVDDAP VASSYVAYRG TSKLAEDAEM KDLKSVIGYI GPHVHFIQYP LRGGELLNQV
AVFESQRYLD GRTAGDIPED WGNPEELDRA YNHCDPFIQD RLDTLWRNNW WQMSDREPLE
NWRIGRMLLL GDAAHAPLQY LASGAVMAME DAEAVALFAA DAARAGNLDW EEVLAEVEAE
RRPRCSRIQT VGRFWGELWH VEGTARLIRN EVFRQADRNG WFIYADWLWG YDASKRAHIA
NPELGEMPQA LKEWRYALLE QK
