ID A0A4T9TIR5_9ACTN Unreviewed; 991 AA.
AC A0A4T9TIR5;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Molybdopterin dinucleotide-binding protein {ECO:0000313|EMBL:TJW11322.1};
GN ORFNames=E5982_03690 {ECO:0000313|EMBL:TJW11322.1};
OS Parvibacter caecicola.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC Coriobacteriaceae; Parvibacter.
OX NCBI_TaxID=747645 {ECO:0000313|EMBL:TJW11322.1, ECO:0000313|Proteomes:UP000309454};
RN [1] {ECO:0000313|EMBL:TJW11322.1, ECO:0000313|Proteomes:UP000309454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM48_B13 {ECO:0000313|EMBL:TJW11322.1,
RC ECO:0000313|Proteomes:UP000309454};
RA Navarre W., Wong E., Huang K.C., Tropini C., Ng K., Yu B.;
RT "Microbes associate with the intestines of laboratory mice.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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:TJW11322.1}.
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DR EMBL; SSTM01000002; TJW11322.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4T9TIR5; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000309454; Unassembled WGS sequence.
DR GO; GO:0018818; F:acetylene hydratase activity; IEA:InterPro.
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; cd02781; MopB_CT_Acetylene-hydratase; 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; 2.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037949; MopB_CT_Acetylene-hydratase.
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 PANTHER; PTHR43598:SF5; DMSO REDUCTASE CHAIN A; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 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; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000309454};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..991
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5020588789"
FT DOMAIN 45..102
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 991 AA; 109816 MW; 82799C3DD2EB5B27 CRC64;
MSKLTMTRRT FTKAAAVTAA ALSVAAPAGV ALAETEVDAK TTGEVKHIRS ACRGCGKMEC
GVWVTVQDGR VIKSEGDESA FQSAGNHCAK GQASLQAAYH PDRLKYPMKR TTPKGENPEW
QRITWEEAYQ TTVDAIHANQ EKYGNETCFF MGGTSRIWAM GPYSALKNCF HTPNGIQANQ
ICKGPRFYAT NLDASNAYSW MEVVGRPRVY VQWGGASELS NYDDSCRTTV DVATRANCHI
LVDPRQTNLG KEADIWVNPR PGTDGVIANC WANVIIENDL IDEMYVRKWM NAPMLVVMEE
TFAPTRSSSA AKSASIITRL LKESDLVEGG ADTRFMVVNE MNGQLSYYET AGCGGWEGEQ
WEPGVWGPGK EANQPGLADT GQTQGFVPDY TPFPDGLYPA LFTEEGGREV TLKDGTKVHV
RTVWENYIDF LQDYTPEKAS EITGVDAEVL KKAAITYATR IDPSTGYGNG GIQYMLALEH
ACNGIQNNRA CDLVAGITGN MDIPGGMRGS TPGWPCMDLA MTAGDSKEMG RFSSEKILGK
ERFVMLGSDC APGWADATSV YDAINTGKPY NVTCGIGQTG DFMNQSNSIY AAENLKKLDF
WCSIDLWQTP CVDMIADIAM PAAHWLELDC IRKSQGSSGA FGATVKAIDP PGEAKNDLEI
VVGIYKAAGV PYFDDAIHGA KWLEGEACVD GCNEVALAGF RIPKWSDYKE EFQKNGWFDS
KVEKPDAWGC YRRYQLGNTP VSGGFPPFPK QMWHQGWNTT THKQEIWSTV LESWLVNGVN
NGGIPVKDQF DGEEFSLKEV FPRFKEAYHG PVTQPELYAD ENSFLMTTGR RQGTYFHSEH
RQLPWCRELW PVPRLEMNPA DAERLGLQQG DWVWIETDKH KIREVVDLYY GIQPGVVNAE
HQWWYPELKQ ADHGYQLSGV NCLLDQYAQD RIIGSSNLRA YGVKVYKATP ENSPFGNPVP
CGDDGTEIIH TCDDPRLKEW LPDYESARGE A
//
