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Database: UniProt
Entry: A4N0P2_HAEIF
LinkDB: A4N0P2_HAEIF
Original site: A4N0P2_HAEIF 
ID   A4N0P2_HAEIF            Unreviewed;       556 AA.
AC   A4N0P2;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   SubName: Full=Biotin sulfoxide reductase {ECO:0000313|EMBL:EDJ87965.1};
GN   ORFNames=CGSHi22121_01502 {ECO:0000313|EMBL:EDJ87965.1};
OS   Haemophilus influenzae 22.1-21.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=374927 {ECO:0000313|EMBL:EDJ87965.1, ECO:0000313|Proteomes:UP000004131};
RN   [1] {ECO:0000313|EMBL:EDJ87965.1, ECO:0000313|Proteomes:UP000004131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22.1-21 {ECO:0000313|EMBL:EDJ87965.1,
RC   ECO:0000313|Proteomes:UP000004131};
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA   Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT   nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(2007).
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; AAZD01000005; EDJ87965.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4N0P2; -.
DR   Proteomes; UP000004131; Unassembled WGS sequence.
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; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   Gene3D; 3.90.55.10; Dimethylsulfoxide Reductase, domain 3; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR041954; CT_DMSOR/BSOR/TMAOR.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR   PANTHER; PTHR43742:SF10; TRIMETHYLAMINE-N-OXIDE REDUCTASE 2; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR   PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          4..293
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          411..532
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   556 AA;  61594 MW;  59F0B02B8571E03B CRC64;
     MLNAEWIPVN TATDVPLMLG IAHTLVEQGK HDKDFLKKYT SGYAKFEEYL LGKTDGQPKT
     AEWAAKICGV PAETIKQLAA DFSSKRTMLM GGWGMQRQRH GEQTHWMLVT LASMLGQIGL
     PGGGFGLSYH YSNGGVPTAT GGIIGSITAS PSGKAGAKTW LDDTSKSAFP LARIADVLLH
     PGKKIQYNGT EITYPDIKAV YWAGGNPFVH HQDTNTLVKA FQKPDVVIVN EVNWTPTARM
     ADIVLPATTS YERNDLTMAG DYSMMSVYPM KQVVPPQFEA KNDYDIFVEL AKRAGVEEQY
     TEGKTEMEWL EEFYNAAFSA ARANRVAMPR FDKFWAENKP LSFEVGEAAK KWVRYGEFRE
     DPLLNPLGTP SGKIEIFSDV IEKMHYNDCK GHPSWMEPEE FAGNVTEEYP LALVTPHPYY
     RLHSQLAHTS LRQKYAVNDR EPVMIHPEDA TARGIKDGDI VRIHSKRGQV LAGAVVTENI
     IKGTVALHEG AWYDPMDLGE SEKPLCKNGC ANVLTRDEGT SKLAQGNSPN TCIVQIEKFT
     GVAPEVTVFK QPKQVA
//
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