MOBA_COMTE
ID MOBA_COMTE Reviewed; 639 AA.
AC Q6SSJ6; Q05KQ5;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=3-hydroxybenzoate 4-monooxygenase;
DE EC=1.14.13.23;
DE AltName: Full=3-hydroxybenzoate 4-hydroxylase;
DE AltName: Full=M-hydroxybenzoate hydroxylase;
GN Name=mobA;
OS Comamonas testosteroni (Pseudomonas testosteroni).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=285;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KH122-3S;
RA Chen R., Chaen H., Hosokawa K.;
RT "Studies on m-hydroxybenzoate 4-hydroxylase I. Purification and
RT properties.";
RL Res. Commun. Biochem. Cell Mol. Biol. 1:304-322(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP MUTAGENESIS OF ASN-227; VAL-257; GLN-292; ALA-400; ASP-416 AND LYS-429.
RC STRAIN=GZ39;
RX PubMed=18417078; DOI=10.1016/j.bbrc.2008.04.032;
RA Chang H.K., Zylstra G.J.;
RT "Examination and expansion of the substrate range of m-hydroxybenzoate
RT hydroxylase.";
RL Biochem. Biophys. Res. Commun. 371:149-153(2008).
RN [3]
RP CRYSTALLIZATION.
RC STRAIN=KH122-3S;
RA Chen R., Oki H., Scott R.P. Jr., Yamaguchi H., Kusunoki M., Matsuura Y.,
RA Chaen H., Tsugita A., Hosokawa K.;
RT "Crystallization and future characterization of meta-hydroxybenzoate 4-
RT hydroxylase from Comamonas testosteroni.";
RL Res. Commun. Biochem. Cell Mol. Biol. 2:253-274(1998).
RN [4]
RP IDENTIFICATION.
RX PubMed=24826896; DOI=10.1371/journal.pone.0097250;
RA Shearer A.G., Altman T., Rhee C.D.;
RT "Finding sequences for over 270 orphan enzymes.";
RL PLoS ONE 9:E97250-E97250(2014).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH FAD, COFACTOR, AND
RP SUBUNIT.
RC STRAIN=KH122-3S;
RX PubMed=17045293; DOI=10.1016/j.jmb.2006.09.031;
RA Hiromoto T., Fujiwara S., Hosokawa K., Yamaguchi H.;
RT "Crystal structure of 3-hydroxybenzoate hydroxylase from Comamonas
RT testosteroni has a large tunnel for substrate and oxygen access to the
RT active site.";
RL J. Mol. Biol. 364:878-896(2006).
CC -!- FUNCTION: Converts 3-hydroxybenzoate (m-hydroxybenzoate), and to a
CC lesser extent p-hydroxybenzoate, to 3,4-dihydroxybenzoate
CC (protocatechuate). Also acts on a number of analogs of 3-
CC hydroxybenzoate substituted in the 2, 4, 5 and 6 positions.
CC {ECO:0000269|PubMed:18417078}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxybenzoate + H(+) + NADPH + O2 = 3,4-dihydroxybenzoate
CC + H2O + NADP(+); Xref=Rhea:RHEA:11480, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16193,
CC ChEBI:CHEBI:36241, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.14.13.23; Evidence={ECO:0000269|PubMed:18417078};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:17045293};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17045293}.
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; AY450844; AAR25885.1; -; Genomic_DNA.
DR EMBL; EF394133; ABN58510.1; -; Genomic_DNA.
DR EMBL; EF394138; ABN58515.1; -; Genomic_DNA.
DR EMBL; AB119008; BAF34928.1; -; Genomic_DNA.
DR RefSeq; WP_003074815.1; NZ_UFXL01000001.1.
DR PDB; 2DKH; X-ray; 1.80 A; A=1-639.
DR PDB; 2DKI; X-ray; 2.50 A; A=1-639.
DR PDBsum; 2DKH; -.
DR PDBsum; 2DKI; -.
DR AlphaFoldDB; Q6SSJ6; -.
DR SMR; Q6SSJ6; -.
DR GeneID; 63998055; -.
DR BRENDA; 1.14.13.2; 1590.
DR BRENDA; 1.14.13.23; 1590.
DR GO; GO:0018668; F:3-hydroxybenzoate 4-monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR Gene3D; 3.40.30.20; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012941; Phe_hydrox_C_dim_dom.
DR InterPro; IPR038220; PHOX_C_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF07976; Phe_hydrox_dim; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; NADP; Oxidoreductase.
FT CHAIN 1..639
FT /note="3-hydroxybenzoate 4-monooxygenase"
FT /id="PRO_0000430458"
FT BINDING 34..64
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17045293"
FT BINDING 73
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17045293"
FT BINDING 166
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17045293"
FT BINDING 212
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17045293"
FT BINDING 269..271
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17045293"
FT BINDING 317
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17045293"
FT BINDING 349
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17045293"
FT BINDING 365
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17045293"
FT MUTAGEN 227
FT /note="N->H: In MobA3-1; able to hydroxylate 3-aminophenol;
FT when associated with R-292 and A-416."
FT /evidence="ECO:0000269|PubMed:18417078"
FT MUTAGEN 257
FT /note="V->A: Broadens the substrate range rendering it able
FT to transform phenol to catechol."
FT /evidence="ECO:0000269|PubMed:18417078"
FT MUTAGEN 292
FT /note="Q->R: In MobA3-1; able to hydroxylate 3-aminophenol;
FT when associated with H-227 and A-416."
FT /evidence="ECO:0000269|PubMed:18417078"
FT MUTAGEN 400
FT /note="A->G: In MobA14-1; able to hydroxylate 3-
FT aminophenol; when associated with R-429."
FT /evidence="ECO:0000269|PubMed:18417078"
FT MUTAGEN 416
FT /note="D->A: In MobA3-1; able to hydroxylate 3-aminophenol;
FT when associated with H-227 and R-292."
FT /evidence="ECO:0000269|PubMed:18417078"
FT MUTAGEN 429
FT /note="K->R: In MobA14-1; able to hydroxylate 3-
FT aminophenol; when associated with G-400."
FT /evidence="ECO:0000269|PubMed:18417078"
FT CONFLICT 112
FT /note="A -> G (in Ref. 1; ABN58515/BAF34928)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="I -> V (in Ref. 1; ABN58515/BAF34928)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="D -> E (in Ref. 1; ABN58515/BAF34928)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="A -> V (in Ref. 1; ABN58515/BAF34928)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="S -> K (in Ref. 1; ABN58515/BAF34928)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="S -> C (in Ref. 1; ABN58515/BAF34928)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="L -> V (in Ref. 1; ABN58515/BAF34928)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="G -> A (in Ref. 1; ABN58515/BAF34928)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="S -> G (in Ref. 1; ABN58515/BAF34928)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="S -> A (in Ref. 1; ABN58515/BAF34928)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="I -> V (in Ref. 1; ABN58515/BAF34928)"
FT /evidence="ECO:0000305"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:2DKH"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:2DKH"
FT HELIX 79..87
FT /evidence="ECO:0007829|PDB:2DKH"
FT HELIX 91..97
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2DKI"
FT STRAND 117..126
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:2DKH"
FT HELIX 140..153
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 163..171
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:2DKH"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 195..205
FT /evidence="ECO:0007829|PDB:2DKH"
FT HELIX 212..216
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 230..239
FT /evidence="ECO:0007829|PDB:2DKH"
FT TURN 242..245
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:2DKH"
FT HELIX 290..301
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 306..317
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:2DKH"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:2DKH"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:2DKH"
FT HELIX 363..380
FT /evidence="ECO:0007829|PDB:2DKH"
FT HELIX 386..389
FT /evidence="ECO:0007829|PDB:2DKH"
FT HELIX 390..409
FT /evidence="ECO:0007829|PDB:2DKH"
FT HELIX 428..442
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:2DKH"
FT HELIX 461..463
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:2DKH"
FT TURN 481..483
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:2DKH"
FT HELIX 489..492
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 499..504
FT /evidence="ECO:0007829|PDB:2DKH"
FT TURN 507..511
FT /evidence="ECO:0007829|PDB:2DKH"
FT HELIX 516..526
FT /evidence="ECO:0007829|PDB:2DKH"
FT HELIX 531..535
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 544..551
FT /evidence="ECO:0007829|PDB:2DKH"
FT HELIX 556..558
FT /evidence="ECO:0007829|PDB:2DKH"
FT HELIX 561..563
FT /evidence="ECO:0007829|PDB:2DKH"
FT HELIX 566..568
FT /evidence="ECO:0007829|PDB:2DKH"
FT TURN 573..576
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 582..585
FT /evidence="ECO:0007829|PDB:2DKH"
FT HELIX 595..598
FT /evidence="ECO:0007829|PDB:2DKH"
FT TURN 603..605
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 607..611
FT /evidence="ECO:0007829|PDB:2DKH"
FT STRAND 615..621
FT /evidence="ECO:0007829|PDB:2DKH"
FT HELIX 626..634
FT /evidence="ECO:0007829|PDB:2DKH"
SQ SEQUENCE 639 AA; 70489 MW; AB056E8831F14E58 CRC64;
MQFHLNGFRP GNPLIAPASP LAPAHTEAVP SQVDVLIVGC GPAGLTLAAQ LAAFPDIRTC
IVEQKEGPME LGQADGIACR TMEMFEAFEF ADSILKEACW INDVTFWKPD PAQPGRIARH
GRVQDTEDGL SEFPHVILNQ ARVHDHYLER MRNSPSRLEP HYARRVLDVK IDHGAADYPV
TVTLERCDAA HAGQIETVQA RYVVGCDGAR SNVRRAIGRQ LVGDSANQAW GVMDVLAVTD
FPDVRYKVAI QSEQGNVLII PREGGHLVRF YVEMDKLDAD ERVASRNITV EQLIATAQRV
LHPYKLDVKN VPWWSVYEIG QRICAKYDDV ADAVATPDSP LPRVFIAGDA CHTHSPKAGQ
GMNFSMQDSF NLGWKLAAVL RKQCAPELLH TYSSERQVVA QQLIDFDREW AKMFSDPAKE
GGQGGVDPKE FQKYFEQHGR FTAGVGTHYA PSLLTGQASH QALASGFTVG MRFHSAPVVR
VSDAKPLQLG HCGKADGRWR LYAFAGQNDL AQPESGLLAL CRFLESDAAS PLRRFTPSGQ
DIDSIFDLRA IFPQAYTEVA LETLPALLLP PKGQLGMIDY EKVFSPDLKN AGQDIFELRG
IDRQQGALVV VRPDQYVAQV LPLGDHAALS AYFESFMRA
