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Database: UniProt
Entry: G2DZN2_9GAMM
LinkDB: G2DZN2_9GAMM
Original site: G2DZN2_9GAMM 
ID   G2DZN2_9GAMM            Unreviewed;       160 AA.
AC   G2DZN2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Adenylylsulfate reductase, beta subunit {ECO:0000313|EMBL:EGV32259.1};
GN   ORFNames=ThidrDRAFT_1495 {ECO:0000313|EMBL:EGV32259.1};
OS   Thiorhodococcus drewsii AZ1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiorhodococcus.
OX   NCBI_TaxID=765913 {ECO:0000313|EMBL:EGV32259.1, ECO:0000313|Proteomes:UP000004200};
RN   [1] {ECO:0000313|EMBL:EGV32259.1, ECO:0000313|Proteomes:UP000004200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AZ1 {ECO:0000313|EMBL:EGV32259.1,
RC   ECO:0000313|Proteomes:UP000004200};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V.,
RA   Frigaard N.-U., Bryant D.A., Woyke T.J.;
RT   "The draft genome of Thiorhodococcus drewsii AZ1.";
RL   Submitted (JUN-2011) 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:EGV32259.1}.
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DR   EMBL; AFWT01000008; EGV32259.1; -; Genomic_DNA.
DR   RefSeq; WP_007040209.1; NZ_AFWT01000008.1.
DR   AlphaFoldDB; G2DZN2; -.
DR   STRING; 765913.ThidrDRAFT_1495; -.
DR   PATRIC; fig|765913.3.peg.1519; -.
DR   eggNOG; COG1146; Bacteria.
DR   OrthoDB; 9781785at2; -.
DR   Proteomes; UP000004200; Unassembled WGS sequence.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 6.20.260.10; Adenylylsulphate reductase, beta subunit, C-terminal domain; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR011802; AprB.
DR   InterPro; IPR022738; AprB_C.
DR   InterPro; IPR038465; APS_reduc_Bsu_C_sf.
DR   NCBIfam; TIGR02060; aprB; 1.
DR   PANTHER; PTHR43687:SF5; 4FE-4S FERREDOXIN-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43687; ADENYLYLSULFATE REDUCTASE, BETA SUBUNIT; 1.
DR   Pfam; PF12139; APS-reductase_C; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          1..30
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          33..62
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   160 AA;  18062 MW;  6D3873BA0EDB5451 CRC64;
     MPTFVYMTRC DGCGQCVDIC PSDIMHIDTT VRRAYNIEPN MCWECYSCVK ACPHNAIDVR
     GYADFAPLGH SVRVRRDEEK GVIAWRIIFR NGEKDMNLLA PITTKPWGTG IPKLADVPAP
     STDMRDSQLL FNEPKYIRLD DGGLHTLESN GLKMKAGVYY
//
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