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Database: UniProt
Entry: F2ASE6_RHOBT
LinkDB: F2ASE6_RHOBT
Original site: F2ASE6_RHOBT 
ID   F2ASE6_RHOBT            Unreviewed;       451 AA.
AC   F2ASE6;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Regulatory protein {ECO:0000313|EMBL:EGF27393.1};
GN   ORFNames=RBWH47_04633 {ECO:0000313|EMBL:EGF27393.1};
OS   Rhodopirellula baltica WH47.
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=991778 {ECO:0000313|EMBL:EGF27393.1, ECO:0000313|Proteomes:UP000006222};
RN   [1] {ECO:0000313|EMBL:EGF27393.1, ECO:0000313|Proteomes:UP000006222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH47 {ECO:0000313|EMBL:EGF27393.1,
RC   ECO:0000313|Proteomes:UP000006222};
RX   PubMed=23273849;
RA   Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., Richter M.,
RA   Achstetter T., Glockner F.O., Harder J.;
RT   "Expression of sulfatases in Rhodopirellula baltica and the diversity of
RT   sulfatases in the genus Rhodopirellula.";
RL   Mar. Genomics 0:0-0(2012).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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:EGF27393.1}.
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DR   EMBL; AFAR01000143; EGF27393.1; -; Genomic_DNA.
DR   RefSeq; WP_007326557.1; NZ_AFAR01000143.1.
DR   AlphaFoldDB; F2ASE6; -.
DR   PATRIC; fig|991778.3.peg.2805; -.
DR   Proteomes; UP000006222; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR   PANTHER; PTHR43014:SF4; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE RCLA-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000350-3};
KW   NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   DOMAIN          6..320
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          342..448
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   BINDING         52
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         174..181
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         197
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         263
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         304
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   DISULFID        43..48
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ   SEQUENCE   451 AA;  48672 MW;  67AA4606D2904040 CRC64;
     MSSEHFDLVV LGTGPSGGTV ATKIAKAGKR VALVDSRTFG GVCALRGCNP KKVYVNAGQL
     VDQIHRGDGK LISDASVKID WKQLHAFKME FTQPVAEKKE QSFQEDGIKT FHGVARFISP
     DTIDVVGTKL TADRFLIATG GRPRELSFDG AEHVTRSDEF LELESMPEHV VFIGGGYISM
     EFAGVVARAG SRVTVIEKNN QILSGFDPDL VNQLTDSLRR HGIRFQMNAE ITGIKKSADG
     HLQVHLANEQ SPIVCGLVVH GAGRVPNIDE LCLSQGEIQH GEKGIAVNQF MQNPTNSRVF
     ATGDCADNGM PRLTPVANED ARIAAKNLFS ETLERTPDYG HVPKVAFTIR SIASVGLSEE
     AARDSNDNLT VLSDDTSSWG SVRKTGPTVA GYKILIDSKT DAILGAHLLG PSAEETINLF
     ALAMKFNLTA TDMKSTLFAF PTFASDVRSM L
//
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