ID A0A2C6M917_9FIRM Unreviewed; 147 AA.
AC A0A2C6M917;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Adenylylsulfate reductase subunit beta {ECO:0000313|EMBL:PHJ38787.1};
GN ORFNames=P378_07220 {ECO:0000313|EMBL:PHJ38787.1};
OS Desulforamulus profundi.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=1383067 {ECO:0000313|EMBL:PHJ38787.1, ECO:0000313|Proteomes:UP000222564};
RN [1] {ECO:0000313|EMBL:PHJ38787.1, ECO:0000313|Proteomes:UP000222564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bs107 {ECO:0000313|EMBL:PHJ38787.1,
RC ECO:0000313|Proteomes:UP000222564};
RA Aullo T., Berlendis S., Lascourreges J.-F., Dessort D., Saint-Laurent S.,
RA Schraauwers B., Mas J., Magot M., Ranchou-Peyruse A.;
RT "Biodegradation of hydrocarbons in the deep terrestrial subsurface :
RT characterization of a microbial consortium composed of two Desulfotomaculum
RT species originating from a deep geological formation.";
RL Submitted (SEP-2013) 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:PHJ38787.1}.
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; AWQQ01000042; PHJ38787.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C6M917; -.
DR OrthoDB; 9807879at2; -.
DR Proteomes; UP000222564; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000222564}.
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 147 AA; 16459 MW; 58A619356B8981B3 CRC64;
MPSFVIAEKC DGCKGQDKTA CMYICPNDLM VLDREKMKAT NRDVSQCWEC YCCVKICPQQ
AIDVRGYADF VPMGASCVPL RSSDSIMWTV KFRNGMLKRF KFPIRTTAEG SAEPAGGYTV
DQENLNDQLL FTEPYSVGTP ELPGMKK
//