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
//