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Database: UniProt
Entry: G2FE27_9GAMM
LinkDB: G2FE27_9GAMM
Original site: G2FE27_9GAMM 
ID   G2FE27_9GAMM            Unreviewed;       128 AA.
AC   G2FE27;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Adenylylsulfate reductase, beta subunit {ECO:0000313|EMBL:EGW55011.1};
DE            EC=2.7.2.8 {ECO:0000313|EMBL:EGW55011.1};
GN   Name=aprB {ECO:0000313|EMBL:EGW55011.1};
GN   ORFNames=TevJSym_ag00890 {ECO:0000313|EMBL:EGW55011.1};
OS   endosymbiont of Tevnia jerichonana (vent Tica).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW55011.1, ECO:0000313|Proteomes:UP000005167};
RN   [1] {ECO:0000313|EMBL:EGW55011.1, ECO:0000313|Proteomes:UP000005167}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA   Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA   Sievert S.M., Schweder T.;
RT   "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT   jerichonana share an identical physiology as revealed by proteogenomic
RT   analyses.";
RL   ISME J. 0:0-0(2011).
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:EGW55011.1}.
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DR   EMBL; AFZB01000007; EGW55011.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2FE27; -.
DR   PATRIC; fig|1049564.3.peg.1160; -.
DR   eggNOG; COG1146; Bacteria.
DR   Proteomes; UP000005167; Unassembled WGS sequence.
DR   GO; GO:0003991; F:acetylglutamate kinase activity; IEA:UniProtKB-EC.
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   Pfam; PF12139; APS-reductase_C; 1.
DR   Pfam; PF00037; Fer4; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005167};
KW   Transferase {ECO:0000313|EMBL:EGW55011.1}.
FT   DOMAIN          15..44
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   128 AA;  14336 MW;  F4516A7E3AADEC72 CRC64;
     MKLDKDGSET GHAMKSFNQE PEQCWECYSC IKICPQQAIE ARPYADIVPM GGSVQPLRGT
     DSIMWTIKFR NGTMKRFKFP IRTTPEGSID PYGNTPAADM AKIAEPGFFN HNQQNGYRAG
     DPSELICK
//
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