DSRA_ARCFU
ID DSRA_ARCFU Reviewed; 418 AA.
AC Q59109;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Sulfite reductase, dissimilatory-type subunit alpha;
DE EC=1.8.99.5 {ECO:0000269|PubMed:20822098, ECO:0000269|PubMed:7691984};
DE AltName: Full=Dissimilatory sulfite reductase subunit alpha;
DE AltName: Full=Hydrogensulfite reductase subunit alpha;
GN Name=dsrA; OrderedLocusNames=AF_0423;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-37; 65-71; 82-99;
RP 124-141; 344-355; 362-368 AND 392-413, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=7691984; DOI=10.1099/00221287-139-8-1817;
RA Dahl C., Kredich N.M., Deutzmann R., Trueper H.G.;
RT "Dissimilatory sulphite reductase from Archaeoglobus fulgidus: physico-
RT chemical properties of the enzyme and cloning, sequencing and analysis of
RT the reductase genes.";
RL J. Gen. Microbiol. 139:1817-1828(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) IN COMPLEX WITH DSRB; IRON-SULFUR
RP (4FE-4S) AND SIROHEME, COFACTOR, SUBUNIT, AND REACTION MECHANISM.
RX PubMed=18495156; DOI=10.1016/j.jmb.2008.04.027;
RA Schiffer A., Parey K., Warkentin E., Diederichs K., Huber H., Stetter K.O.,
RA Kroneck P.M.H., Ermler U.;
RT "Structure of the dissimilatory sulfite reductase from the
RT hyperthermophilic archaeon Archaeoglobus fulgidus.";
RL J. Mol. Biol. 379:1063-1074(2008).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH DSRB; IRON-SULFUR
RP (4FE-4S); SIROHEME AND HYDROGENSULFITE, CATALYTIC ACTIVITY, SUBUNIT,
RP COFACTOR, AND REACTION MECHANISM.
RX PubMed=20822098; DOI=10.1021/bi100781f;
RA Parey K., Warkentin E., Kroneck P.M., Ermler U.;
RT "Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus
RT fulgidus.";
RL Biochemistry 49:8912-8921(2010).
CC -!- FUNCTION: Catalyzes the reduction of sulfite to sulfide. This is the
CC terminal oxidation reaction in sulfate respiration.
CC {ECO:0000269|PubMed:7691984}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[DsrC protein]-disulfide + 2 A + 3 H2O + hydrogen sulfide =
CC [DsrC protein]-dithiol + 2 AH2 + H(+) + sulfite;
CC Xref=Rhea:RHEA:47008, Rhea:RHEA-COMP:11722, Rhea:RHEA-COMP:11723,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:17499, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058; EC=1.8.99.5;
CC Evidence={ECO:0000269|PubMed:20822098, ECO:0000269|PubMed:7691984};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[DsrC protein]-S-sulfanyl-L-cysteine/L-cysteine + 3 A + 3 H2O
CC = [DsrC protein]-disulfide + 3 AH2 + 2 H(+) + sulfite;
CC Xref=Rhea:RHEA:47020, Rhea:RHEA-COMP:11722, Rhea:RHEA-COMP:11724,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:50058, ChEBI:CHEBI:61963; EC=1.8.99.5;
CC Evidence={ECO:0000269|PubMed:20822098, ECO:0000269|PubMed:7691984};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:18495156, ECO:0000269|PubMed:20822098};
CC Note=Binds 2 [4Fe-4S] clusters per subunit.
CC {ECO:0000269|PubMed:18495156, ECO:0000269|PubMed:20822098};
CC -!- COFACTOR:
CC Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC Evidence={ECO:0000269|PubMed:18495156, ECO:0000269|PubMed:20822098};
CC Note=Binds 1 siroheme per subunit. {ECO:0000269|PubMed:18495156,
CC ECO:0000269|PubMed:20822098};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Highly thermostable. Inactive towards methylviologen below 55 degrees
CC Celsius.;
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC {ECO:0000269|PubMed:18495156, ECO:0000269|PubMed:20822098}.
CC -!- SUBCELLULAR LOCATION: Membrane. Note=Although the protein complex is
CC found in the soluble fraction it may be membrane-associated in vivo.
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DR EMBL; M95624; AAB17213.1; -; Genomic_DNA.
DR EMBL; AE000782; AAB90812.1; -; Genomic_DNA.
DR PIR; G69302; G69302.
DR RefSeq; WP_010877930.1; NC_000917.1.
DR PDB; 3MM5; X-ray; 1.80 A; A/D=1-418.
DR PDB; 3MM6; X-ray; 1.90 A; A/D=1-418.
DR PDB; 3MM7; X-ray; 1.90 A; A/D=1-418.
DR PDB; 3MM8; X-ray; 2.28 A; A/D=1-418.
DR PDB; 3MM9; X-ray; 2.10 A; A/D=1-418.
DR PDB; 3MMA; X-ray; 2.30 A; A/D=1-418.
DR PDB; 3MMB; X-ray; 2.30 A; A/D=1-418.
DR PDB; 3MMC; X-ray; 2.04 A; A/D=1-418.
DR PDBsum; 3MM5; -.
DR PDBsum; 3MM6; -.
DR PDBsum; 3MM7; -.
DR PDBsum; 3MM8; -.
DR PDBsum; 3MM9; -.
DR PDBsum; 3MMA; -.
DR PDBsum; 3MMB; -.
DR PDBsum; 3MMC; -.
DR AlphaFoldDB; Q59109; -.
DR SMR; Q59109; -.
DR STRING; 224325.AF_0423; -.
DR EnsemblBacteria; AAB90812; AAB90812; AF_0423.
DR GeneID; 24793961; -.
DR KEGG; afu:AF_0423; -.
DR eggNOG; arCOG02057; Archaea.
DR HOGENOM; CLU_660112_0_0_2; -.
DR OMA; MHCLNVM; -.
DR OrthoDB; 58856at2157; -.
DR PhylomeDB; Q59109; -.
DR BioCyc; MetaCyc:MON-12500; -.
DR BRENDA; 1.8.99.5; 414.
DR EvolutionaryTrace; Q59109; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0018551; F:hydrogensulfite reductase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.413.10; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR011806; DsrA.
DR InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR InterPro; IPR045169; NO2/SO3_Rdtase_4Fe4S_prot.
DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR PANTHER; PTHR11493; PTHR11493; 1.
DR Pfam; PF01077; NIR_SIR; 1.
DR Pfam; PF03460; NIR_SIR_ferr; 1.
DR SUPFAM; SSF55124; SSF55124; 1.
DR SUPFAM; SSF56014; SSF56014; 1.
DR TIGRFAMs; TIGR02064; dsrA; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Direct protein sequencing; Heme; Iron; Iron-sulfur;
KW Membrane; Metal-binding; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7691984"
FT CHAIN 2..418
FT /note="Sulfite reductase, dissimilatory-type subunit alpha"
FT /id="PRO_0000080025"
FT DOMAIN 277..305
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 176
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18495156,
FT ECO:0000269|PubMed:20822098, ECO:0007744|PDB:3MM5,
FT ECO:0007744|PDB:3MMC"
FT BINDING 182
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18495156,
FT ECO:0000269|PubMed:20822098, ECO:0007744|PDB:3MM5,
FT ECO:0007744|PDB:3MMC"
FT BINDING 220
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18495156,
FT ECO:0000269|PubMed:20822098, ECO:0007744|PDB:3MM5,
FT ECO:0007744|PDB:3MMC"
FT BINDING 224
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18495156,
FT ECO:0000269|PubMed:20822098, ECO:0007744|PDB:3MM5,
FT ECO:0007744|PDB:3MMC"
FT BINDING 224
FT /ligand="siroheme"
FT /ligand_id="ChEBI:CHEBI:60052"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305|PubMed:18495156,
FT ECO:0000305|PubMed:20822098"
FT BINDING 267
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18495156,
FT ECO:0000269|PubMed:20822098, ECO:0007744|PDB:3MM5,
FT ECO:0007744|PDB:3MMC"
FT BINDING 286
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18495156,
FT ECO:0000269|PubMed:20822098, ECO:0007744|PDB:3MM5,
FT ECO:0007744|PDB:3MMC"
FT BINDING 289
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18495156,
FT ECO:0000269|PubMed:20822098, ECO:0007744|PDB:3MM5,
FT ECO:0007744|PDB:3MMC"
FT BINDING 292
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18495156,
FT ECO:0000269|PubMed:20822098, ECO:0007744|PDB:3MM5,
FT ECO:0007744|PDB:3MMC"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 18..34
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 44..58
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:3MM5"
FT TURN 84..88
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 110..123
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 147..156
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 201..205
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 232..241
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 247..254
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:3MM5"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:3MM5"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 304..312
FT /evidence="ECO:0007829|PDB:3MM5"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 326..332
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 339..355
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 362..369
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 371..377
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:3MM5"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:3MM5"
FT HELIX 407..415
FT /evidence="ECO:0007829|PDB:3MM5"
SQ SEQUENCE 418 AA; 47525 MW; AC12A7BFDF27EEEF CRC64;
MSETPLLDEL EKGPWPSFVK EIKKTAELME KAAAEGKDVK MPKGARGLLK QLEISYKDKK
THWKHGGIVS VVGYGGGVIG RYSDLGEQIP EVEHFHTMRI NQPSGWFYST KALRGLCDVW
EKWGSGLTNF HGSTGDIIFL GTRSEYLQPC FEDLGNLEIP FDIGGSGSDL RTPSACMGPA
LCEFACYDTL ELCYDLTMTY QDELHRPMWP YKFKIKCAGC PNDCVASKAR SDFAIIGTWK
DDIKVDQEAV KEYASWMDIE NEVVKLCPTG AIKWDGKELT IDNRECVRCM HCINKMPKAL
KPGDERGATI LIGGKAPFVE GAVIGWVAVP FVEVEKPYDE IKEILEAIWD WWDEEGKFRE
RIGELIWRKG MREFLKVIGR EADVRMVKAP RNNPFMFFEK DELKPSAYTE ELKKRGMW
