ID F4B5N2_ACIHW Unreviewed; 704 AA.
AC F4B5N2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:AEE94456.1};
GN OrderedLocusNames=Ahos_1573 {ECO:0000313|EMBL:AEE94456.1};
OS Acidianus hospitalis (strain W1).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Acidianus.
OX NCBI_TaxID=933801 {ECO:0000313|EMBL:AEE94456.1, ECO:0000313|Proteomes:UP000008458};
RN [1] {ECO:0000313|EMBL:AEE94456.1, ECO:0000313|Proteomes:UP000008458}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W1 {ECO:0000313|EMBL:AEE94456.1,
RC ECO:0000313|Proteomes:UP000008458};
RX PubMed=21607549; DOI=10.1007/s00792-011-0379-y;
RA You X.Y., Liu C., Wang S.Y., Jiang C.Y., Shah S.A., Prangishvili D.,
RA She Q., Liu S.J., Garrett R.A.;
RT "Genomic analysis of Acidianus hospitalis W1 a host for studying
RT crenarchaeal virus and plasmid life cycles.";
RL Extremophiles 15:487-497(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W1;
RA You X.Y., Liu C., Wang S.Y., Jiang C.Y., Shah S.A., Prangishvili D.,
RA Liu S.J., Garrett R.A.;
RT "Genomic analyses of Acidianus hospitalis W1 a host for studying
RT crenarchaeal virus and plasmid life cycles.";
RL Extremophiles 0:0-0(2011).
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP002535; AEE94456.1; -; Genomic_DNA.
DR RefSeq; WP_013776371.1; NC_015518.1.
DR AlphaFoldDB; F4B5N2; -.
DR STRING; 933801.Ahos_1573; -.
DR GeneID; 10601074; -.
DR KEGG; aho:Ahos_1573; -.
DR eggNOG; arCOG01491; Archaea.
DR HOGENOM; CLU_000422_13_3_2; -.
DR OrthoDB; 23466at2157; -.
DR Proteomes; UP000008458; 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 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 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.
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 1..50
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|SMART:SM00926"
SQ SEQUENCE 704 AA; 79967 MW; 68E88C63269DEA55 CRC64;
MAFLRCYMCK NACGIIATVE GKVVRVAANR NHPQPGICGR GAAGPYLLTH PDRLKSPLTR
EGDQLVPTSW EKALDEVTKR LKELLDEGHP EYLAITYHDY GKELLERFAA LYGTPNLIGH
ESVCHGPRTV AAELVLGAEG PRSIDPDYPN SKFVVFIGRN PLEGIVPDIV RRIEEGRKNG
MKIAVIDPRK SAIAQRYADR WIPIRPGTDT AFLLSVIYYM IKNGMYDEDF LKMYSNASLL
VYEDDLSPAN EYSDKLIYEG QKDGRRVATA FYLLMKEGEK VYPRLTYITG ATYDDVKYIA
ENLWENRPSA VIDDGWHTSF STDSTYTWMS AFIINAMIGN LDKKGGLIFS KKPRIKLYEE
NKAKVKRIDK IRYPLTYAAF QEVYRAILTG SPYPIKALMV VGTNLDGRDP NSDLVRRALS
KLDFLVVVDV MPSDVTDYAD VVLAESTYLE RDELPLPVGW TLEAWVDIHQ KAVEPYYDTK
PLWWILLELE RRLGLANDTF DSLQDMILSK LGINKEELYS KGCVKIPTEI YEVYPYKKEL
NTPSGKVEIY STILHEHGYY PLPTYIEKNV MPREDDEFYL TSGHTLYHTQ DSITFDIPTL
IKLAPENPVT INKKRAEKLG IKDNDEVELI SLTTGQRVRC KVRVTDDIRE DTAFTYFGFG
RHSKGEKFAY GHGFDVNSLI SDQITDPISG SIAQSLNIVK IRKV
//