APRB_MEGG1
ID APRB_MEGG1 Reviewed; 167 AA.
AC T2G899; D2YW41; S5VNU5;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Adenylylsulfate reductase subunit beta {ECO:0000303|PubMed:19820092, ECO:0000303|PubMed:2158885, ECO:0000312|EMBL:AGS82786.1, ECO:0000312|EMBL:AGW12371.1, ECO:0000312|PDB:3GYX};
DE Short=AdoPSO(4) reductase subunit B {ECO:0000303|PubMed:2158885};
DE AltName: Full=Adenosine 5'-phosphosulfate reductase subunit beta {ECO:0000303|PubMed:19820092};
DE Short=APSR subunit B {ECO:0000303|PubMed:19820092};
GN Name=aprB {ECO:0000303|PubMed:19820092, ECO:0000312|EMBL:AGS82786.1,
GN ECO:0000312|EMBL:AGW12371.1};
GN ORFNames=DGI_0458 {ECO:0000312|EMBL:AGW12371.1};
OS Megalodesulfovibrio gigas (strain ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM
OS B-1759) (Desulfovibrio gigas).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Megalodesulfovibrio.
OX NCBI_TaxID=1121448;
RN [1] {ECO:0000312|EMBL:AGS82786.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759
RC {ECO:0000312|EMBL:AGS82786.1};
RX PubMed=23974026; DOI=10.1128/jb.00411-13;
RA Morais-Silva F.O., Santos C.I., Rodrigues R., Pereira I.A.,
RA Rodrigues-Pousada C.;
RT "Roles of HynAB and Ech, the only two hydrogenases found in the model
RT sulfate reducer Desulfovibrio gigas.";
RL J. Bacteriol. 195:4753-4760(2013).
RN [2] {ECO:0000312|EMBL:AGW12371.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759
RC {ECO:0000312|EMBL:AGW12371.1};
RA Morais-Silva F.O., Rezende A.M., Pimentel C., Resende D.M., Santos C.I.,
RA Clemente C., de Oliveira L.M., da Silva S.M., Costa D.A., Varela-Raposo A.,
RA Horacio E.C.A., Matos M., Flores O., Ruiz J.C., Rodrigues-Pousada C.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|PDB:3GYX, ECO:0007744|PDB:3GYX}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-167, X-RAY CRYSTALLOGRAPHY (3.20
RP ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (4FE-4S) AND APRA, FUNCTION,
RP CATALYTIC ACTIVITY OF THE ADENYLYLSULFATE REDUCTASE, COFACTOR, SUBUNIT,
RP DOMAINS, AND SITES.
RC STRAIN=ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759
RC {ECO:0000303|PubMed:19820092};
RX PubMed=19820092; DOI=10.1128/jb.00583-09;
RA Chiang Y.L., Hsieh Y.C., Fang J.Y., Liu E.H., Huang Y.C., Chuankhayan P.,
RA Jeyakanthan J., Liu M.Y., Chan S.I., Chen C.J.;
RT "Crystal structure of Adenylylsulfate reductase from Desulfovibrio gigas
RT suggests a potential self-regulation mechanism involving the C terminus of
RT the beta-subunit.";
RL J. Bacteriol. 191:7597-7608(2009).
RN [4]
RP CATALYTIC ACTIVITY OF THE ADENYLYLSULFATE REDUCTASE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=7240092; DOI=10.1128/jb.147.1.161-169.1981;
RA Odom J.M., Peck H.D. Jr.;
RT "Localization of dehydrogenases, reductases, and electron transfer
RT components in the sulfate-reducing bacterium Desulfovibrio gigas.";
RL J. Bacteriol. 147:161-169(1981).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY OF THE ADENYLYLSULFATE REDUCTASE, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, EPR AND MOESSBAUER SPECTROSCOPY OF
RP THE ADENYLYLSULFATE REDUCTASE, AND REDOX TITRATIONS.
RC STRAIN=ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759
RC {ECO:0000303|PubMed:2158885};
RX PubMed=2158885; DOI=10.1111/j.1432-1033.1990.tb15447.x;
RA Lampreia J., Moura I., Teixeira M., Peck H.D. Jr., Legall J., Huynh B.H.,
RA Moura J.J.;
RT "The active centers of adenylylsulfate reductase from Desulfovibrio gigas.
RT Characterization and spectroscopic studies.";
RL Eur. J. Biochem. 188:653-664(1990).
CC -!- FUNCTION: Iron-sulfur cluster subunit of the adenylylsulfate reductase
CC which catalyzes reversibly the reduction of adenosine 5'-phosphosulfate
CC (APS) to sulfite and AMP during dissimilatory sulfate reduction. The
CC iron-sulfur cluster 2 is thought to accept electrons from a still
CC unknown electron donor and transfer electrons to the iron-sulfur
CC cluster 1 of this protein and then onto the FAD of AprA.
CC {ECO:0000269|PubMed:19820092, ECO:0000269|PubMed:2158885}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:19820092, ECO:0000269|PubMed:2158885};
CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000269|PubMed:19820092,
CC ECO:0000269|PubMed:2158885};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.4 for the adenylylsulfate reductase.
CC {ECO:0000269|PubMed:2158885};
CC Redox potential:
CC E(0) is about 0 mV for 4Fe-4S cluster 1 and is estimated to be lower
CC than -400 mV for a fully reduced 4Fe-4S cluster 2.
CC {ECO:0000269|PubMed:2158885};
CC -!- SUBUNIT: Heterodimer composed of AprA and AprB (PubMed:19820092,
CC PubMed:2158885). The heterodimers can dimerize to form heterotetramers
CC (PubMed:2158885). {ECO:0000269|PubMed:19820092,
CC ECO:0000269|PubMed:2158885}.
CC -!- INTERACTION:
CC T2G899; T2G6Z9: aprA; NbExp=3; IntAct=EBI-6409220, EBI-6409227;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7240092}.
CC -!- DOMAIN: Consists of three sections from the N- to the C-terminus: [4Fe-
CC 4S] cluster-binding domain, beta-sheet and C-terminal tail. The beta-
CC sheet and the C-terminal tail interact with AprA to stabilize the
CC AprA/AprB heterodimer. {ECO:0000269|PubMed:19820092}.
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DR EMBL; KF113859; AGS82786.1; -; Genomic_DNA.
DR EMBL; CP006585; AGW12371.1; -; Genomic_DNA.
DR RefSeq; WP_021759002.1; NZ_AUBO01000012.1.
DR PDB; 3GYX; X-ray; 3.20 A; B/D/F/H/J/L=2-167.
DR PDBsum; 3GYX; -.
DR AlphaFoldDB; T2G899; -.
DR SMR; T2G899; -.
DR IntAct; T2G899; 1.
DR STRING; 1121448.DGI_0458; -.
DR KEGG; dgg:DGI_0458; -.
DR PATRIC; fig|1121448.10.peg.455; -.
DR HOGENOM; CLU_142910_0_0_7; -.
DR OMA; CWECYNC; -.
DR SABIO-RK; T2G899; -.
DR Proteomes; UP000016587; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0019420; P:dissimilatory sulfate reduction; IDA:UniProtKB.
DR GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
DR Gene3D; 6.20.260.10; -; 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 Pfam; PF12139; APS-reductase_C; 1.
DR Pfam; PF13187; Fer4_9; 1.
DR TIGRFAMs; TIGR02060; aprB; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Cytoplasm; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Reference proteome; Transport.
FT CHAIN 1..167
FT /note="Adenylylsulfate reductase subunit beta"
FT /id="PRO_0000434042"
FT DOMAIN 1..35
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 38..67
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 10
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19820092,
FT ECO:0007744|PDB:3GYX"
FT BINDING 13
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19820092,
FT ECO:0007744|PDB:3GYX"
FT BINDING 21
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19820092,
FT ECO:0007744|PDB:3GYX"
FT BINDING 25
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19820092,
FT ECO:0007744|PDB:3GYX"
FT BINDING 47
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19820092,
FT ECO:0007744|PDB:3GYX"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19820092,
FT ECO:0007744|PDB:3GYX"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19820092,
FT ECO:0007744|PDB:3GYX"
FT BINDING 57
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19820092,
FT ECO:0007744|PDB:3GYX"
FT SITE 48
FT /note="Important for the electron transfer from the iron-
FT sulfur cluster 1 to the FAD of AprA"
FT /evidence="ECO:0000305"
FT SITE 152
FT /note="Important for interaction with AprA at the substrate
FT channel entrance"
FT /evidence="ECO:0000269|PubMed:19820092"
FT SITE 159
FT /note="Important for interaction with AprA at the substrate
FT channel entrance"
FT /evidence="ECO:0000269|PubMed:19820092"
FT SITE 163
FT /note="Important for interaction with AprA at the substrate
FT channel entrance"
FT /evidence="ECO:0000269|PubMed:19820092"
FT CONFLICT 4
FT /note="F -> Y (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:3GYX"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 20..24
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:3GYX"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:3GYX"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:3GYX"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:3GYX"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:3GYX"
SQ SEQUENCE 167 AA; 18445 MW; 4CE816D5DD932C50 CRC64;
MPTFVDPSKC DGCKGGEKTA CMYICPNDLM ILDPEEMKAF NQEPEACWEC YSCIKICPQG
AITARPYADF APMGGTCIPL RGSEDIMWTI KFRNGSVKRF KFPIRTTPEG SIKPFEGKPE
AGDLENELLF TETALTVPQV ALGQKAQIAD AETSQCWFDL PCEGGNR
