ID A0A0F5ZQE3_9GAMM Unreviewed; 842 AA.
AC A0A0F5ZQE3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=trimethylamine-N-oxide reductase {ECO:0000256|ARBA:ARBA00011885};
DE EC=1.7.2.3 {ECO:0000256|ARBA:ARBA00011885};
GN ORFNames=RN22_23675 {ECO:0000313|EMBL:KKD57966.1};
OS Grimontia sp. AD028.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Grimontia.
OX NCBI_TaxID=1581149 {ECO:0000313|EMBL:KKD57966.1, ECO:0000313|Proteomes:UP000033732};
RN [1] {ECO:0000313|EMBL:KKD57966.1, ECO:0000313|Proteomes:UP000033732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD028 {ECO:0000313|EMBL:KKD57966.1,
RC ECO:0000313|Proteomes:UP000033732};
RA Adrian T.-G.-S., Chan K.-G.;
RT "Genome sequencing of Grimontia sp. AD028.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKD57966.1}.
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; LASY01000165; KKD57966.1; -; Genomic_DNA.
DR RefSeq; WP_046308357.1; NZ_LASY01000165.1.
DR AlphaFoldDB; A0A0F5ZQE3; -.
DR PATRIC; fig|1581149.3.peg.1242; -.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000033732; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0009033; F:trimethylamine-N-oxide reductase activity; IEA:UniProtKB-EC.
DR CDD; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 1.
DR CDD; cd02769; MopB_DMSOR-BSOR-TMAOR; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR Gene3D; 3.90.55.10; Dimethylsulfoxide Reductase, domain 3; 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 NCBIfam; TIGR00509; bisC_fam; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR PANTHER; PTHR43742:SF4; TRIMETHYLAMINE-N-OXIDE REDUCTASE 1; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF18364; Molybdopterin_N; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 53..93
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 97..567
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 686..806
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 842 AA; 93463 MW; 7EDEEA163DD3DD2E CRC64;
MATEKQQGIS RRRFLSGMLT ASAGVVIGSS LLAPRKAMAA TEAKNTFSGE VIHGSHWGAF
RAKVENGIWV DTVAFENDPH PTSMLNGVRE VVYNPSRVKY PMVRIDWLKH GWKSDTSQRG
DNRFVRVPWS QALDFFHHEL ERVQNTYGPS ALYAGHSGWQ SCGKFNTAGT MMQRAISLHG
TYLAKVGDYS TGSAQVVLPY VAGAMEVYEQ QTSWPLVLEN AKNIVIWGSD PIKNLQVGWL
VPDHSVYGYY QQLAEKVKAG EINVIHVDPV KNESYKFFGG SQVAVNPQTD VPLMLAIAHT
LYTEKLYDEQ FLADYTTGFD KFVPYLTGEK DGVAKTPEWA AEICGIPADQ IRELARTMAN
GRTQIIAGWC LQRMQHGEQY AWMIVVLAAM LGQIGLPGGG FGFGWHYNDA GTITSAGPLM
SGFSSVTGVD PIHSGSYNGY SSYIPVARFV DCIENPGTTI QFNGHSVKFP HMKMAIFCGN
NPFHHHQDRN RMIKAWRNLE TVVSVEHQWT ATCRFADIVL PATTTYERND IEQFGNHSNK
GIIAMKQIVE PMFEAKDDFD IFRELCTRYG REEAFTGGKT KMEWIEEIYN GARLQGRGIG
VRMPNFVKFW EEEQFIAFPE GSEWVRHAAF RKEPDLEPLG TASGLIEIYC KTIADMGYDD
CQGHPMWFEK VERSHGGPKS KQYPIHLQSC HPNHRLHSQL CSSDDHRGTY AVAGREPCYI
STADAKVRGI QSGDIVRVFN DRGQVLAGAV VTDDYMSGVC RIHEGAWYAP LEGGKPGTLC
TYGDPNVLTV DIGTSKLAQA TSAHTALVEI EKYTGKVPAV TGFSGPIAVD DVNPLFPAMD
IA
//
