ID A0A261UXS0_9BORD Unreviewed; 586 AA.
AC A0A261UXS0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Sulfurase {ECO:0000313|EMBL:OZI66367.1};
GN ORFNames=CAL28_01070 {ECO:0000313|EMBL:OZI66367.1};
OS Bordetella genomosp. 11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1416808 {ECO:0000313|EMBL:OZI66367.1, ECO:0000313|Proteomes:UP000215767};
RN [1] {ECO:0000313|EMBL:OZI66367.1, ECO:0000313|Proteomes:UP000215767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU8856 {ECO:0000313|EMBL:OZI66367.1,
RC ECO:0000313|Proteomes:UP000215767};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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:OZI66367.1}.
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DR EMBL; NEVS01000001; OZI66367.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261UXS0; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000215767; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06184; flavohem_like_fad_nad_binding; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.33.20; PK beta-barrel domain-like; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR005302; MoCF_Sase_C.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR005163; YiiM-like_3-alpha_domain.
DR PANTHER; PTHR30212:SF2; PROTEIN YIIM; 1.
DR PANTHER; PTHR30212; UNCHARACTERIZED; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF03475; YiiM_3-alpha; 1.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714}.
FT DOMAIN 29..164
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT DOMAIN 235..340
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 586 AA; 62520 MW; A59E2E615323E5D4 CRC64;
MARLVSVNVG LPRDVAWKGR TVHTGIWKYP VYGRCRVGRL NLEGDGQGDL AGHGGEQRAV
LVYQVEAYRH WEAQLGRKDL VHGQFGENFT VEGLADAEVC IGDRYRIGTA LFEVTQPRVT
CYRVGIRMNE PRMPALLTAS GLPGFYLRVL REGEVGPGDE IAKVGEATDR LTVAAVNALL
YSPHHPREQL ERALRVDALS PGWRGSFKAL LEQSNALPGG NAGLAPAAAR RPVAPGFRPL
AVTAMDNECD DVVSLTLRAT DGQPLPAHLP GQYVVLRLRT AADAPPLFRS YSLSGADSAQ
SYRISVKVET NGAAGNYLRT RIEQGALLDV SAPRGTFALQ PGDGPVVLLS AGIGATPVLA
MLHALAAAHT KRRVLWLYAA RDGRHHPFAA EARGLVRSLP HASSHVRYSR PGPEDRVGQD
FDATGRLSAA ALREVGIPPG ADIYLCGPPA FMNDMKEALA SLQVPPARIH AETFNGGDTL
TPGIAPAAAR MPHPPENASA DGPLISFARS GIATRWDPSA YQSILELAEA CDVPVRWSCR
AGVCHNCESG LVSGDVAYQP APLDAPAAGN VLICCARPRG DVVIDL
//
