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Entry: H2IRF4_RAHAC
LinkDB: H2IRF4_RAHAC
Original site: H2IRF4_RAHAC 
ID   H2IRF4_RAHAC            Unreviewed;       818 AA.
AC   H2IRF4;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family {ECO:0000313|EMBL:AEX51390.1};
GN   OrderedLocusNames=Rahaq2_1511 {ECO:0000313|EMBL:AEX51390.1};
OS   Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 /
OS   NCIMB 13365 / CIP 78.65).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Rahnella.
OX   NCBI_TaxID=745277 {ECO:0000313|EMBL:AEX51390.1, ECO:0000313|Proteomes:UP000009010};
RN   [1] {ECO:0000313|EMBL:AEX51390.1, ECO:0000313|Proteomes:UP000009010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC   CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RX   PubMed=22582378; DOI=10.1128/JB.00380-12;
RA   Martinez R.J., Bruce D., Detter C., Goodwin L.A., Han J., Han C.S.,
RA   Held B., Land M.L., Mikhailova N., Nolan M., Pennacchio L., Pitluck S.,
RA   Tapia R., Woyke T., Sobecky P.A.;
RT   "Complete Genome Sequence of Rahnella aquatilis CIP 78.65.";
RL   J. Bacteriol. 194:3020-3021(2012).
RN   [2] {ECO:0000313|Proteomes:UP000009010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC   CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sobecky P.,
RA   Martinez R., Woyke T.;
RT   "Complete sequence of chromosome of Rahnella aquatilis CIP 78.65.";
RL   Submitted (JAN-2012) 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   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR   EMBL; CP003244; AEX51390.1; -; Genomic_DNA.
DR   RefSeq; WP_015696612.1; NZ_JMPO01000015.1.
DR   AlphaFoldDB; H2IRF4; -.
DR   STRING; 745277.Rahaq2_1511; -.
DR   GeneID; 61511610; -.
DR   KEGG; raq:Rahaq2_1511; -.
DR   PATRIC; fig|745277.3.peg.1453; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_3_6; -.
DR   OrthoDB; 9815647at2; -.
DR   Proteomes; UP000009010; Chromosome.
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; cd02794; MopB_CT_DmsA-EC; 1.
DR   CDD; cd02770; MopB_DmsA-EC; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.12440; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
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; IPR006311; TAT_signal.
DR   InterPro; IPR049754; YnfE.
DR   NCBIfam; TIGR02166; dmsA_ynfE; 1.
DR   NCBIfam; NF041885; selenate_YnfE; 1.
DR   PANTHER; PTHR43742:SF7; DIMETHYL SULFOXIDE REDUCTASE CHAIN YNFE-RELATED; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000009010};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          59..120
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   818 AA;  90911 MW;  C086E7D4E6D7E539 CRC64;
     MSEIKPEITT LTSGISRRTL MKTSTLAGLA IAAGGVSLPF GRKALAQFAN EAKHSVSADK
     VVWGACSVNC GSRCALRLHV RDDEVYWVET DNTGQDIYGD HQVRACLRGR SIRRRMNHPE
     RLNYPMKRVG KRGEGKFKRI SWEEAFDEIA NNLKRIVAKY GNEAVYINYT SGIVGGNITR
     SSPYASLVAR LMNCYGGFLS HYGTYSTAQI ACAMPYTYGS NDGNSTSDIE NSKLIVLFGN
     NPAETRMSGG GITYYLEQAR QRSNARMIVI DPRYTDTAAG REDEWIPIRP GTDAALVAGL
     AHVLITENMV DQAFLDAYCV GYDEKTLPAD APANSHYKAY ILGQGEDAIA KTPEWASRIT
     GIPADRIVKL AREIGQAKPA YISQGWGPQR QANGELTSRA IAMLPILTGN VGINGGNSGA
     RESTYTITIE RMPVLENPVK TQISCFSWTD AIARGPQMTA TKDGVRGKDK LDVPIKFIWN
     YAGNTITNQH SDINKTHDIL QDDAQCEMIV VLENFMTSSA KYADILLPDL MTVEQEDIIP
     NDYAGNMGYL IFIQPATSAK FERKGIYEVM SEVARRLGPD VFNKFTEGRT QREWLQYLYA
     KMLAKDPALP AYEELREMGI YKRKDPAGHF VAYKKFRQDP HANPLKTPSG KIEIYSSALA
     KIAREWELQK DETISPLPVY ASTFEGWDDP KRSQFPLQMF GFHYKARTHS TYGNIDVLQA
     SCRQEVWINP MDAKTRGIEN GDKVKVFNDR GEVRVAAKVT PRIMPGVVAM GQGAWHQANM
     SGDRIDHGAC MNTLTTQRPS PLAKGNPQHT NLIQIEKI
//
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