ID Q9L768_DESDE Unreviewed; 162 AA.
AC Q9L768;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Adenylylsulfate reductase beta subunit {ECO:0000313|EMBL:AAF36689.1};
GN Name=aprA {ECO:0000313|EMBL:AAF36689.1};
OS Desulfovibrio desulfuricans.
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=876 {ECO:0000313|EMBL:AAF36689.1};
RN [1] {ECO:0000313|EMBL:AAF36689.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Essex 6 {ECO:0000313|EMBL:AAF36689.1};
RX PubMed=10802060; DOI=10.1016/S0014-5793(00)01500-3;
RA Fritz G., Buchert T., Huber H., Stetter K.O., Kroneck P.M.;
RT "Adenylylsulfate reductases from archaea and bacteria are 1:1 alphabeta-
RT heterodimeric iron-sulfur flavoenzymes--high similarity of molecular
RT properties emphasizes their central role in sulfur metabolism.";
RL FEBS Lett. 473:63-66(2000).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF226708; AAF36689.1; -; Genomic_DNA.
DR RefSeq; WP_022658830.1; NZ_CP072608.1.
DR AlphaFoldDB; Q9L768; -.
DR GeneID; 72383821; -.
DR BRENDA; 1.8.99.2; 1905.
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; PF13187; Fer4_9; 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..35
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 38..67
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 162 AA; 17995 MW; 3C228D5CE0E13FC2 CRC64;
MPTFVDPSKC DGCKGGEKTA CMYICPNDLM ILDSEEMKAY NQEPDACWEC YSCVKICPQG
AITARPYADF APMGGTCIPM RSADSIMWTV KFRNGNVKRF KFPIRTTPEG SIKPFEGHPE
GANIEDELLF TETALVAPKT ALGKKFDVKD ANKTFTCMEH GR
//
