TORA_SHEMA
ID TORA_SHEMA Reviewed; 829 AA.
AC O87948;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=torA;
OS Shewanella massilia.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=76854;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 32-61, AND
RP INDUCTION.
RX PubMed=9813127; DOI=10.1006/jmbi.1998.2155;
RA Dos Santos J.P., Iobbi-Nivol C., Couillault C., Giordano G., Mejean V.;
RT "Molecular analysis of the trimethylamine N-oxide (TMAO) reductase
RT respiratory system from a Shewanella species.";
RL J. Mol. Biol. 284:421-433(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH OXIDIZED MO-BIS-MGD,
RP AND COFACTOR.
RX PubMed=9813128; DOI=10.1006/jmbi.1998.2156;
RA Czjzek M., Dos Santos J.P., Pommier J., Giordano G., Mejean V., Haser R.;
RT "Crystal structure of oxidized trimethylamine N-oxide reductase from
RT Shewanella massilia at 2.5-A resolution.";
RL J. Mol. Biol. 284:435-447(1998).
CC -!- FUNCTION: Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an
CC anaerobic reaction coupled to energy-yielding reactions.
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:0000269|PubMed:9813128};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000269|PubMed:9813128};
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- INDUCTION: By TMAO and DMSO. {ECO:0000269|PubMed:9813127}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
CC -!- MISCELLANEOUS: Although torA is induced by both TMAO and DMSO, only
CC TMAO is used as a natural substrate.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AJ006085; CAA06851.1; -; Genomic_DNA.
DR PDB; 1TMO; X-ray; 2.50 A; A=1-829.
DR PDBsum; 1TMO; -.
DR AlphaFoldDB; O87948; -.
DR SMR; O87948; -.
DR KEGG; ag:CAA06851; -.
DR BRENDA; 1.7.2.3; 5705.
DR EvolutionaryTrace; O87948; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
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 CDD; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
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 InterPro; IPR011887; TorA.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF18364; Molybdopterin_N; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR02164; torA; 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; Direct protein sequencing; Metal-binding; Molybdenum;
KW Oxidoreductase; Periplasm; Signal.
FT SIGNAL 1..31
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:9813127"
FT CHAIN 32..829
FT /note="Trimethylamine-N-oxide reductase"
FT /id="PRO_0000019157"
FT BINDING 180
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 STRAND 41..45
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 95..100
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 119..136
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:1TMO"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 158..167
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 184..191
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 236..248
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 263..268
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 280..293
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 299..305
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 309..317
FT /evidence="ECO:0007829|PDB:1TMO"
FT TURN 318..321
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 327..334
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 338..350
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:1TMO"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 368..381
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:1TMO"
FT TURN 398..401
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 435..438
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 442..447
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 452..454
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 456..461
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 467..472
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 475..478
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 482..489
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 493..501
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 504..507
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 510..515
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 518..520
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 523..527
FT /evidence="ECO:0007829|PDB:1TMO"
FT TURN 529..531
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 534..538
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 551..561
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 565..569
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 574..589
FT /evidence="ECO:0007829|PDB:1TMO"
FT TURN 590..592
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 598..604
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 606..608
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 619..623
FT /evidence="ECO:0007829|PDB:1TMO"
FT TURN 625..627
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 631..640
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 642..645
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 665..668
FT /evidence="ECO:0007829|PDB:1TMO"
FT TURN 669..673
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 676..679
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 684..687
FT /evidence="ECO:0007829|PDB:1TMO"
FT TURN 691..693
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 695..698
FT /evidence="ECO:0007829|PDB:1TMO"
FT TURN 699..701
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 708..711
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 713..718
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 726..730
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 735..742
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 750..752
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 769..772
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 777..780
FT /evidence="ECO:0007829|PDB:1TMO"
FT HELIX 783..785
FT /evidence="ECO:0007829|PDB:1TMO"
FT TURN 794..796
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 805..810
FT /evidence="ECO:0007829|PDB:1TMO"
FT STRAND 820..822
FT /evidence="ECO:0007829|PDB:1TMO"
SQ SEQUENCE 829 AA; 92362 MW; 6F58A59E8C41CF1F CRC64;
MNRRDFLKGI ASSSFVVLGG SSVLTPLNAL AKAGINEDEW LTTGSHFGAF KMKRKNGVIA
EVKPFDLDKY PTDMINGIRG MVYNPSRVRY PMVRLDFLLK GHKSNTHQRG DFRFVRVTWD
KALTLFKHSL DEVQTQYGPS GLHAGQTGWR ATGQLHSSTS HMQRAVGMHG NYVKKIGDYS
TGAGQTILPY VLGSTEVYAQ GTSWPLILEH SDTIVLWSND PYKNLQVGWN AETHESFAYL
AQLKEKVKQG KIRVISIDPV VTKTQAYLGC EQLYVNPQTD VTLMLAIAHE MISKKLYDDK
FIQGYSLGFE EFVPYVMGTK DGVAKTPEWA APICGVEAHV IRDLAKTLVK GRTQFMMGWC
IQRQQHGEQP YWMAAVLATM IGQIGLPGGG ISYGHHYSSI GVPSSGAAAP GAFPRNLDEN
QKPLFDSSDF KGASSTIPVA RWIDAILEPG KTIDANGSKV VYPDIKMMIF SGNNPWNHHQ
DRNRMKQAFH KLECVVTVDV NWTATCRFSD IVLPACTTYE RNDIDVYGAY ANRGILAMQK
MVEPLFDSLS DFEIFTRFAA VLGKEKEYTR NMGEMEWLET LYNECKAANA GKFEMPDFAT
FWKQGYVHFG DGEVWTRHAD FRNDPEINPL GTPSGLIEIF SRKIDQFGYD DCKGHPTWME
KTERSHGGPG SDKHPIWLQS CHPDKRLHSQ MCESREYRET YAVNGREPVY ISPVDAKARG
IKDGDIVRVF NDRGQLLAGA VVSDNFPKGI VRIHEGAWYG PVGKDGSTEG GAEVGALCSY
GDPNTLTLDI GTSKLAQACS AYTCLVEFEK YQGKVPKVSS FDGPIEVEI
