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
//