TORZ_HAEIN
ID TORZ_HAEIN Reviewed; 825 AA.
AC P44798;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Trimethylamine-N-oxide reductase;
DE Short=TMAO reductase;
DE Short=Trimethylamine oxidase;
DE EC=1.7.2.3;
DE Flags: Precursor;
GN Name=torZ; Synonyms=bisC; OrderedLocusNames=HI_0643;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an
CC anaerobic reaction coupled to energy-yielding reactions. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome c] + H2O + trimethylamine = 2 Fe(II)-
CC [cytochrome c] + 3 H(+) + trimethylamine N-oxide;
CC Xref=Rhea:RHEA:24236, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15724,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:58389; EC=1.7.2.3;
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
CC -!- CAUTION: Was originally assigned to be a biotin sulfoxide reductase
CC hence the original gene designation of bisC.
CC {ECO:0000305|PubMed:7542800}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L42023; AAC22303.1; -; Genomic_DNA.
DR PIR; H64083; H64083.
DR RefSeq; NP_438803.1; NC_000907.1.
DR RefSeq; WP_010869026.1; NC_000907.1.
DR PDB; 7L5I; X-ray; 1.73 A; A=41-825.
DR PDB; 7L5S; X-ray; 2.09 A; A=41-825.
DR PDBsum; 7L5I; -.
DR PDBsum; 7L5S; -.
DR AlphaFoldDB; P44798; -.
DR SMR; P44798; -.
DR STRING; 71421.HI_0643; -.
DR TCDB; 5.A.3.4.4; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR EnsemblBacteria; AAC22303; AAC22303; HI_0643.
DR KEGG; hin:HI_0643; -.
DR PATRIC; fig|71421.8.peg.672; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_6; -.
DR OMA; DQMPKHV; -.
DR PhylomeDB; P44798; -.
DR BioCyc; HINF71421:G1GJ1-678-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0030151; F:molybdenum ion binding; IBA:GO_Central.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0050626; F:trimethylamine-N-oxide reductase (cytochrome c) activity; IEA:UniProtKB-EC.
DR GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
DR CDD; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006658; BisC.
DR InterPro; IPR041954; CT_DMSOR/BSOR/TMAOR.
DR InterPro; IPR041460; Molybdopterin_N.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF18364; Molybdopterin_N; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR00509; bisC_fam; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Molybdenum; Oxidoreductase; Periplasm;
KW Reference proteome; Signal.
FT SIGNAL 1..40
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 41..825
FT /note="Trimethylamine-N-oxide reductase"
FT /id="PRO_0000019166"
FT BINDING 187
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:7L5I"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:7L5S"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 126..143
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 191..199
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 211..217
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 256..263
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 283..296
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 302..308
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 312..319
FT /evidence="ECO:0007829|PDB:7L5I"
FT TURN 320..324
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 330..337
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 341..353
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:7L5I"
FT TURN 368..370
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 371..384
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 393..396
FT /evidence="ECO:0007829|PDB:7L5I"
FT TURN 401..404
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:7L5S"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 443..448
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 453..456
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 468..473
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 476..479
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 483..489
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 492..502
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 511..516
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 519..521
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 524..529
FT /evidence="ECO:0007829|PDB:7L5I"
FT TURN 530..532
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 535..539
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 552..562
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 566..570
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 575..592
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 600..606
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 616..620
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 625..629
FT /evidence="ECO:0007829|PDB:7L5I"
FT TURN 631..633
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 641..646
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 648..653
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 668..670
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 671..673
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 676..678
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 680..683
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 688..691
FT /evidence="ECO:0007829|PDB:7L5I"
FT TURN 695..697
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 699..703
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 711..714
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 716..720
FT /evidence="ECO:0007829|PDB:7L5I"
FT TURN 721..723
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 729..733
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 738..745
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 747..749
FT /evidence="ECO:0007829|PDB:7L5S"
FT STRAND 753..756
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 774..777
FT /evidence="ECO:0007829|PDB:7L5I"
FT HELIX 780..782
FT /evidence="ECO:0007829|PDB:7L5I"
FT TURN 791..793
FT /evidence="ECO:0007829|PDB:7L5I"
FT STRAND 802..807
FT /evidence="ECO:0007829|PDB:7L5I"
SQ SEQUENCE 825 AA; 91053 MW; 4254287D42B45E5B CRC64;
MKKNNVNEQR RDFLKKTSLG VAGSALSGGM VGVVSKSAVA KEAEMKTVVT AAHWGSIGVV
VQDGKVVKSG PAIEPAVPNE LQTVVADQLY SERRVKCPMV RKGFLANPGK SDTTMRGRDE
WVRVSWDEAL DLVHNQLKRV RDEHGSTGIF AGSYGWFSCG SLHASRTLLQ RYMNATGGFV
GHKGDYSTGA AQVIMPHVLG TIEVYEQQTS WESILESSDI IVLWSANPLT TMRIAWMSTD
QKGIEYFKKF QASGKRIICI DPQKSETCQM LNAEWIPVNT ATDVPLMLGI AHTLVEQGKH
DKDFLKKYTS GYAKFEEYLL GKTDGQPKTA EWAAKICGVP AETIKQLAAD FASKRTMLMG
GWGMQRQRHG EQTHWMLVTL ASMLGQIGLP GGGFGLSYHY SNGGVPTATG GIIGSITASP
SGKAGAKTWL DDTSKSAFPL ARIADVLLHP GKKIQYNGTE ITYPDIKAVY WAGGNPFVHH
QDTNTLVKAF QKPDVVIVNE VNWTPTARMA DIVLPATTSY ERNDLTMAGD YSMMSVYPMK
QVVPPQFEAK NDYDIFVELA KRAGVEEQYT EGKTEMEWLE EFYNAAFSAA RANRVAMPRF
DKFWAENKPL SFEAGEAAKK WVRYGEFRED PLLNPLGTPS GKIEIFSDVV EKMNYNDCKG
HPSWMEPEEF AGNVTEEYPL ALVTPHPYYR LHSQLAHTSL RQKYAVNDRE PVMIHPEDAA
ARGIKDGDIV RIHSKRGQVL AGAAVTENII KGTVALHEGA WYDPMYLGES EKPLCKNGCA
NVLTRDEGTS KLAQGNSPNT CIVQIEKFIG VAPEVTVFKQ PKQVA
