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Database: UniProt
Entry: I2B6U7_SHIBC
LinkDB: I2B6U7_SHIBC
Original site: I2B6U7_SHIBC 
ID   I2B6U7_SHIBC            Unreviewed;      1023 AA.
AC   I2B6U7; K6VFZ4;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Putative molybdopterin oxidoreductase family protein {ECO:0000313|EMBL:AFJ46251.1};
GN   OrderedLocusNames=EBL_c11470 {ECO:0000313|EMBL:AFJ46251.1};
OS   Shimwellia blattae (strain ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 /
OS   CDC 9005-74) (Escherichia blattae).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shimwellia.
OX   NCBI_TaxID=630626 {ECO:0000313|EMBL:AFJ46251.1, ECO:0000313|Proteomes:UP000001955};
RN   [1] {ECO:0000313|EMBL:AFJ46251.1, ECO:0000313|Proteomes:UP000001955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 / CDC 9005-74
RC   {ECO:0000313|Proteomes:UP000001955};
RX   PubMed=22843577; DOI=10.1128/JB.00829-12;
RA   Brzuszkiewicz E., Waschkowitz T., Wiezer A., Daniel R.;
RT   "Complete genome sequence of the B12-producing Shimwellia blattae strain
RT   DSM 4481, isolated from a cockroach.";
RL   J. Bacteriol. 194:4436-4436(2012).
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; CP001560; AFJ46251.1; -; Genomic_DNA.
DR   RefSeq; WP_002441152.1; NZ_BAHA01000012.1.
DR   AlphaFoldDB; I2B6U7; -.
DR   STRING; 630626.EBL_c11470; -.
DR   KEGG; ebt:EBL_c11470; -.
DR   PATRIC; fig|630626.3.peg.1106; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_008235_0_0_6; -.
DR   OrthoDB; 9815647at2; -.
DR   Proteomes; UP000001955; Chromosome.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02780; MopB_CT_Tetrathionate_Arsenate-R; 1.
DR   CDD; cd02758; MopB_Tetrathionate-Ra; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 2.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR037946; MopB_CT_Tetrathionate.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR041929; Tetrathionate-R_A_N.
DR   PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 1.
DR   PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 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; 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:UP000001955};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          71..155
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   1023 AA;  110932 MW;  0E235B7A5FBFA70A CRC64;
     MAELSRRQWL KIGVAVGGFA AFGLSYRDVA QRAVDGLVNG TSGKVTRDKI FANALEPEGR
     IQGGWQQNPD QAISMTQCFG CWTLCGLRVR VDKKANRVLR IAGNPWHPLS HEAPFDSAMP
     FAQAMARLGG EGGMPSRSTA CARGATLAEG LYSPQRILTP MKRAGKRGEG KWQRISFEQL
     IAEVVEGGDL FGEGHVDGLR AIRDLTTPVD ARHPDYGPRA NQLMVTNAGD DGRDGFLRRF
     AQHSFGSKNF GAHGAYCGLA YRAGSGALLG DLDKNPHVKP DWENVEFALF MGTSPAQSGN
     PFKRQARQLA SARLRDTFRY VVVAPALPLT TVQADSHGRW LALRPGSDSA LAMAMIRWII
     ENNRYTAEYL SMTSREAMLR AGEKSWTNAC WLVITDEQHP RAGQHLTTSL LSGEASGNDE
     PLVISEAGEL VPVSQCDRGA LLVTRQITLH DGSSVTVKSS FQCLADSACR FTIAQYSQQC
     GVPQAQIIAL AQAFTSHGRK AAVITHGGMM SGNGFYNAWS VMMLNVLLGN MSLSGGVFVG
     GGKFNGEVNG PCYNFEQFPG KVAPRGMNIA RSKADYARSP EYQEKVARGQ APWPAKAPWY
     PFVAGQLTEL LPSALAGYPY PLKAWISNMT NPLYGVPGLR GIIDAQLRDP QRLPLFIAID
     AFMNETTAFA DYIVPDTHNF ESWGFSTPWA GVATKTTTAR WPVVSAATAK TAQGEPVSME
     AFCIAVARRM GLPGFGDNAI PDSQGEMQGL HRAEDYYLRV AANIAFAGQK PLPPADEQDI
     ALSGVERIFP AIRTTLKPAE ALPVAFLYSR GGRFAPPETG RKAGLVGAEW VKPLQIWNPQ
     VAAYKYALTG ERYSGCPTWY PARLSDGRAL EALYPPARWP LQLISFKSNL MSSSTGVTER
     LHRVKPAGLV AINPQDGKRF GLQHGDRARI RTPGGQLEVQ ISLLAGVMPG VIAIEHGYGH
     KESGARSWWL DGEQVAGQHY AGAGINLNDL GFADPTRKIP GPWLDWVTGA AVRQGLPAMI
     EKV
//
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