Database: SPTrEMBLEntry: TMOA_PSEME
LinkDB: TMOA_PSEME
Original site: TMOA_PSEME
ID TMOA_PSEME Reviewed; 500 AA.
AC Q00456;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 24-NOV-2009, entry version 45.
DE RecName: Full=Toluene-4-monooxygenase system protein A;
DE EC=1.14.13.-;
GN Name=tmoA;
OS Pseudomonas mendocina.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=300;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-14.
RC STRAIN=KR1;
RX MEDLINE=91358306; PubMed=1885512;
RA Yen K.-M., Karl M.R., Blatt L.M., Simon M.J., Winter R.B.,
RA Fausset P.R., Lu H.S., Harcourt A.A., Chen K.K.;
RT "Cloning and characterization of a Pseudomonas mendocina KR1 gene
RT cluster encoding toluene-4-monooxygenase.";
RL J. Bacteriol. 173:5315-5327(1991).
CC -!- FUNCTION: Hydroxylates toluene to form p-cresol.
CC -!- COFACTOR: FAD.
CC -!- COFACTOR: Fe(2+).
CC -!- PATHWAY: Xenobiotic degradation; toluene degradation.
CC -!- SUBUNIT: The multicomponent enzyme toluene-4-monooxygenase is
CC formed by the tmoA, tmoB, tmoC, tmoD, tmoE and tmoF polypeptides.
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DR EMBL; M65106; AAA25999.1; -; Genomic_DNA.
DR PDB; 3DHG; X-ray; 1.85 A; A/D=1-500.
DR PDB; 3DHH; X-ray; 1.94 A; A=1-500.
DR PDB; 3DHI; X-ray; 1.68 A; A=1-500.
DR PDB; 3GE3; X-ray; 1.52 A; A=1-500.
DR PDB; 3GE8; X-ray; 2.19 A; A/D=1-500.
DR PDB; 3I5J; X-ray; 1.90 A; A=1-500.
DR PDB; 3I63; X-ray; 2.09 A; A=1-500.
DR PDBsum; 3DHG; -.
DR PDBsum; 3DHH; -.
DR PDBsum; 3DHI; -.
DR PDBsum; 3GE3; -.
DR PDBsum; 3GE8; -.
DR PDBsum; 3I5J; -.
DR PDBsum; 3I63; -.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR InterPro; IPR009078; Ferritin/RR-like.
DR InterPro; IPR003430; Phenol_Hydrox.
DR InterPro; IPR012348; Ribncl_red_rel.
DR InterPro; IPR007029; YHS.
DR Gene3D; G3DSA:1.10.620.20; Ribncl_red_rel; 1.
DR Pfam; PF02332; Phenol_Hydrox; 1.
DR Pfam; PF04945; YHS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism;
KW Direct protein sequencing; FAD; Flavoprotein; Iron; Monooxygenase;
KW Oxidoreductase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 500 Toluene-4-monooxygenase system protein A.
FT /FTId=PRO_0000072599.
FT HELIX 6 13
FT STRAND 21 23
FT HELIX 25 28
FT TURN 31 33
FT HELIX 41 46
FT HELIX 55 66
FT HELIX 70 75
FT TURN 76 78
FT HELIX 81 84
FT HELIX 90 96
FT HELIX 105 108
FT HELIX 114 117
FT HELIX 124 128
FT HELIX 132 136
FT HELIX 140 146
FT TURN 147 151
FT HELIX 153 156
FT HELIX 157 160
FT HELIX 161 163
FT HELIX 167 179
FT HELIX 185 191
FT HELIX 192 196
FT HELIX 201 205
FT HELIX 209 214
FT HELIX 218 234
FT HELIX 241 247
FT HELIX 251 272
FT HELIX 276 280
FT HELIX 283 285
FT HELIX 290 297
FT HELIX 302 308
FT HELIX 317 332
FT HELIX 339 341
FT STRAND 342 344
FT HELIX 352 361
FT HELIX 372 381
FT HELIX 385 388
FT TURN 398 400
FT STRAND 417 420
FT STRAND 425 428
FT HELIX 431 439
FT HELIX 441 444
FT HELIX 450 455
FT TURN 468 470
FT HELIX 476 478
FT TURN 483 486
FT HELIX 487 491
SQ SEQUENCE 500 AA; 57982 MW; D6BD8D541614726D CRC64;
MAMHPRKDWY ELTRATNWTP SYVTEEQLFP ERMSGHMGIP LEKWESYDEP YKTSYPEYVS
IQREKDAGAY SVKAALERAK IYENSDPGWI STLKSHYGAI AVGEYAAVTG EGRMARFSKA
PGNRNMATFG MMDELRHGQL QLFFPHEYCK KDRQFDWAWR AYHSNEWAAI AAKHFFDDII
TGRDAISVAI MLTFSFETGF TNMQFLGLAA DAAEAGDYTF ANLISSIQTD ESRHAQQGGP
ALQLLIENGK REEAQKKVDM AIWRAWRLFA VLTGPVMDYY TPLEDRSQSF KEFMYEWIIG
QFERSLIDLG LDKPWYWDLF LKDIDELHHS YHMGVLDWRT TAWWNPAAGV TPEERDWLEE
KYPGWNKRWG RCWDVITENV LNDRMDLVSP ETLPSVCNMS QIPLVGVPGD DWNIEVFSLE
HNGRLYHFGS EVDRWVFQQD PVQYQNHMNI VDRFLAGQIQ PMTLEGALKY MGFQSIEEMG
KDAHDFAWAD KCKPAMKKSA
//
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