ID A0A423UIA0_9ACTN Unreviewed; 914 AA.
AC A0A423UIA0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=4Fe-4S Mo/W bis-MGD-type domain-containing protein {ECO:0000259|PROSITE:PS51669};
GN ORFNames=DMP12_11005 {ECO:0000313|EMBL:ROT88751.1};
OS Gordonibacter urolithinfaciens.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Gordonibacter.
OX NCBI_TaxID=1335613 {ECO:0000313|EMBL:ROT88751.1, ECO:0000313|Proteomes:UP000285258};
RN [1] {ECO:0000313|Proteomes:UP000285258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27213 {ECO:0000313|Proteomes:UP000285258};
RA Danylec N., Stoll D.A., Doetsch A., Huch M.;
RT "Genome Sequencing of selected type strains of the family
RT Eggerthellaceae.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:ROT88751.1}.
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DR EMBL; QIBW01000014; ROT88751.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423UIA0; -.
DR Proteomes; UP000285258; Unassembled WGS sequence.
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:InterPro.
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; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-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.
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}.
FT DOMAIN 15..72
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 914 AA; 102401 MW; 5B79D32FD9618CF9 CRC64;
MRNVENAQTG TEGETRKVYA GCRSCHLNCP VWVTVKDGRA VKVEGDPKLG PPNMGKACVR
ASEAIQFEYS PTRLRYPLKR AGKRGEGKWE RVSWDQAVDE IAAKIHEMVE KHGAETFVLP
GRTGRHDMGW VAHRIARTIG TPNNYYGAIQ VCYLPQFHEQ VNYGFYTATG GGSAATKCHV
SFSAEQAYAW PIQAQTIMAN KENGMKLIVV DPVQGVYASK ADEWVPVRPG TDVGLIMGMA
KVIIDKGLYD KDYVVRWSNA PFLVRGDTGG LLLESDIVEG GSDKRFMVWD EKEDRLKYWD
AEEIQWEGGP SGKAHYDHLV ELFEKNKTST EKSPAADLPD SIMPALFGEH EVELCTRGGK
ITCIPAFQML ANNVAEWTPE HTESITGVPA DQVERVATMI GTLKPVDINQ GMQYMSTNVS
QYVNAINVLK IITGSVDVAG GNVLGAFYPV TPHAFPSELD LSWADGLPLE QKRKRLGYYT
HRVGCGYAWE EMVKWQPIRP QNADGAMLFP DLTSVMEAAE TGRPYPVHGI IAISSNWLMH
DPTLARWLKL LEDETKIELH VVTDVVMTPT AEMADYVLPA VTWMERNFLN FGTGGGSSPL
HQAYNKAVEP LCEARHDYDF GAMLSKALGK YDKRYVEGRL NHEWTNHWAG EYGKFWPADT
IDGQRDLLSR EFLGMPFEDV LKRRVVAVPG ADTPPSTERF LIAGKFPTDT GKANLFSTIH
QKCGYPPLPV YVEPAESLLS RPDLAKDYPL VGSYGKRQAG FFHSEFRQLP WTREMTRTPD
VFINPETAAQ FGVAENDWIW VESPPTGGRA PYNKIMGKVS FRFMVAPGIV SYSQHAWWRP
EKTVEEELHG AFEWNTEALI EVENNCPETG SGGYRSQICR IYKATEEDIA RYRPEITREQ
LEALMPMTPE ECAK
//
