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Database: UniProt
Entry: A0A1Q9LEQ4_9PSEU
LinkDB: A0A1Q9LEQ4_9PSEU
Original site: A0A1Q9LEQ4_9PSEU 
ID   A0A1Q9LEQ4_9PSEU        Unreviewed;       676 AA.
AC   A0A1Q9LEQ4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:OLR90449.1};
GN   ORFNames=BJP25_27785 {ECO:0000313|EMBL:OLR90449.1};
OS   Actinokineospora bangkokensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinokineospora.
OX   NCBI_TaxID=1193682 {ECO:0000313|EMBL:OLR90449.1, ECO:0000313|Proteomes:UP000186040};
RN   [1] {ECO:0000313|EMBL:OLR90449.1, ECO:0000313|Proteomes:UP000186040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=44EHW {ECO:0000313|EMBL:OLR90449.1,
RC   ECO:0000313|Proteomes:UP000186040};
RA   Greule A., Intra B., Flemming S., Rommel M.G., Panbangred W., Bechthold A.;
RT   "The Draft Genome Sequence of Actinokineospora bangkokensis 44EHWT reveals
RT   the biosynthetic pathway of antifungal compounds Thailandins with unusual
RT   extender unit butylmalonyl-CoA.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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:OLR90449.1}.
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DR   EMBL; MKQR01000026; OLR90449.1; -; Genomic_DNA.
DR   RefSeq; WP_075977122.1; NZ_MKQR01000026.1.
DR   AlphaFoldDB; A0A1Q9LEQ4; -.
DR   STRING; 1193682.BJP25_27785; -.
DR   OrthoDB; 7376058at2; -.
DR   Proteomes; UP000186040; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster 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   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   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   PANTHER; PTHR43105:SF14; POSSIBLE OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE 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; 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   4: Predicted;
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:ARBA00022485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186040}.
FT   DOMAIN          1..58
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   676 AA;  73292 MW;  A06B75B2A8E7208F CRC64;
     MASTRLITCN LCEACCGLQV EVEQDRVTSV SGDPRDPLSR GHLCPKGVAI GDVHADGKRL
     RTPVRKTATG WQEIGWDAAL DEVATRLADA RERHGRNSVA VYLGNPTAHS LGALTHGTAF
     FGMLRTRNRY SATSVDQLPH HLAAYLLYGH QLLLPIPDID RTDHFLLVGG NPLVSNGSLM
     TVPDFANRRK ELRARGGKFV VLDPRRTETA KVADEHHFVR PGTDAALLLA LVRTVLHEGL
     ATPPPYVDGV AELTEAVAGF TPEWAAPITG VDAGTIERLA REFATAERAV AHGRTGVSMQ
     RHGAVCQWAV QVLNAITGNL DRPGGALATR PAVDILKMVG PGHFGVWRSR VRGLPEFAGE
     LPVSVLAEEI ETPGEGQVKA AVVHAGNPVL STPDGKRLAK ALGQLDFLVA IDIKVTETSE
     HADIVLPPTT LLERDHYDLI FHALAVRDTA RYSPPAIAKP ADARHDWEIF RDLGLRYAKR
     VKTPLATRLR LRLRPTVLLD LLLRVGPHKL TLRKLRKNPS GVDLGPLAPS FPHRLRTKDK
     RVQIAPEMML DALAAVRDMT AEDGLLLIGR RHLRANNSWM NDVARLTRGR PRHHLLMHPK
     DLADNGLVDG ADVLVRSAVG SVRVPVTASE DVMPGVVSLP HGYRGTSAND LTDPAVVDEV
     SGNAVLNGVP VHVTPV
//
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