ID A9BSG1_DELAS Unreviewed; 727 AA.
AC A9BSG1;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:ABX33775.1};
GN OrderedLocusNames=Daci_1130 {ECO:0000313|EMBL:ABX33775.1};
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX33775.1, ECO:0000313|Proteomes:UP000000784};
RN [1] {ECO:0000313|EMBL:ABX33775.1, ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT defined pairs of heterotrophic bacteria.";
RL Appl. Environ. Microbiol. 70:4053-4063(2004).
RN [2] {ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-2007) 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; CP000884; ABX33775.1; -; Genomic_DNA.
DR AlphaFoldDB; A9BSG1; -.
DR STRING; 398578.Daci_1130; -.
DR KEGG; dac:Daci_1130; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_4; -.
DR Proteomes; UP000000784; 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:InterPro.
DR CDD; cd02766; MopB_3; 1.
DR CDD; cd02786; MopB_CT_3; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 1.
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; IPR037920; YoaE_C.
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.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000000784}.
FT DOMAIN 46..103
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 727 AA; 79563 MW; E6818F72B1DDD639 CRC64;
MQDRHRPLPV TAFSRFPGFS RFFRKVPTLS ETAATMSSAT PPVQATSQVL GACPHDCPDT
CSLVTTVEDG IAKRVQGNPA HPHTGGVLCA KVSKYTERSY HPERVLTPLR RVGPKGSGQF
EPVGWDEALA DIAARLQSLA ARDPETILPY SYAGTMGLVQ GESMDRRFFH QLGASLLDRT
ICSSAGGEAL NLTYGGKLGM RVEHFTESRL ILIWGSNSIG SSLHFWRYAL EAKRNGARLV
CIDPRKTETA DKCHEHLQLL PGTDAALALA LMHELITHGW LDHDYIARHT LGWEELKARA
LQWPPERAAQ VCGLPVEQIR QLERDYGTTT PAAIRLNYGV QRARGGGNAV RAIACLPALV
GAWRHRAGGL LLSASGALPA QRARLQMPHL LGERRPRTIN MSTIGDALLH EGGNGFGPRV
DAIVVYNSNP VAVAPESAKV VAGFARENLF TVVLEQFMTD TADLADYVLP ATTQIEHWDI
HGSYGHTDVL LNRPAIAPLG QARSNGQIFR DLAAHMARHD DAFAAAHFQT GDEQLCREAF
EGRGVDFNEL LDKGFATLAL PEAPFAEGGF ATPSGRCEFT SAELARRGMD PLPDYLPNYE
TAETDARYPL AMISPPARNF LNSSFVNVKS LRTMEGRPLV ELHPDDAAPR GVAEGDRVRV
FNDRGSYECH ATLNGRARRG VVNGLGIWWR KHGDNGTNVN ELTHQRLTDL GRAPSFYDCA
VQVQRLA
//
