ID Q1ZSV7_PHOAS Unreviewed; 820 AA.
AC Q1ZSV7;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=Putative anaerobic dimethyl sulfoxide reductase, subunit A {ECO:0000313|EMBL:EAS64870.1};
GN ORFNames=VAS14_04103 {ECO:0000313|EMBL:EAS64870.1};
OS Photobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain S14 /
OS CCUG 15956)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=314292 {ECO:0000313|EMBL:EAS64870.1, ECO:0000313|Proteomes:UP000001603};
RN [1] {ECO:0000313|EMBL:EAS64870.1, ECO:0000313|Proteomes:UP000001603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14 {ECO:0000313|EMBL:EAS64870.1,
RC ECO:0000313|Proteomes:UP000001603};
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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:EAS64870.1}.
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; AAOJ01000002; EAS64870.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1ZSV7; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_6; -.
DR Proteomes; UP000001603; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0009389; F:dimethyl sulfoxide reductase activity; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR CDD; cd02770; MopB_DmsA-EC; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.12440; -; 2.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR011888; Anaer_DMSO_reductase.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR NCBIfam; TIGR02166; dmsA_ynfE; 1.
DR PANTHER; PTHR43742:SF3; DIMETHYL SULFOXIDE REDUCTASE DMSA; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
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 54..116
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 820 AA; 91638 MW; 626EAE366EDC7C0B CRC64;
MSYKIWDNNE CKVSRRNFVK GGTALSTLAL ATSGMTLPFS KKVQAKETLP KPDEKIVWSA
CTIDCGSRCP LRMHVIDGEI KWVETDNTGK DVFNHEHQVR ACLRGRSMRR RVYNPDRLKY
PLKRIGKRGE GKFKRISWDE ALDTIAASLS KTIHKYGNDA VYINYGTGTL GGTVTKSWSP
SETLIARLMN LKGGYLNHYG DYSTGSLAAI SGYLYGDYMS TNGIDDIANA DLCVFFGNNP
AETRMSGGGN IHNYMETEKR SNTRIIVIDP RYTDTACGRE NQWIPIRQGT DAALCAGIAH
VLITENKVNQ DFLDKYCVGY DEKTLPLSAP KNGSYKDYIL GHGDDNTPKT PQWASQITGI
PEDDIIKLAR EIGDAKRLYL SQGWGIQRSS NGEQACKAVA MLPILCGQVG LQGGSTGMRE
GDHTYPFVRF PTLKNPVKAT IPFFLWTDAI TRYKELTPTR DGLRGVEQLQ NPIKFIWAYA
SNTLINQHAN INRTKQILED DKACEMIVVI ENHMTASAKY ADIILPDCTA SEQADFCMDG
AGGMMPYFIF ASQVIKPRFE CRPIYDIMSD LAKRLGVEQA FTEGRSQEDW LKWMYEQTRL
QNNDPDLPNY ETMKSQGIYK KQYDRPFVAL ESFRKDPIAN PLGTPSGKIE IYSEQLAEIA
TKWDLKDDEH ITPISEYHPS FDGWDSPHRK QFPLQMTGFH FKGRVHSTYG NVALLKAAIP
QEIWINPIDA GKRGIKNGDL VLVQSRFGET QVGAKVTPRV MPGVTAMGDG AWYAPNKKGI
DMNGALNTLT NSRPTPLAKA NPSHTNLVEI TLLKSMGVEA
//
