ID   DSVA_NITV2              Reviewed;         437 AA.
AC   P45574; Q46581;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-SEP-2026, entry version 147.
DE   RecName: Full=Sulfite reductase, dissimilatory-type subunit alpha;
DE   AltName: Full=Desulfoviridin subunit alpha;
DE   AltName: Full=Dissimilatory sulfite reductase subunit alpha {ECO:0000303|PubMed:18829451};
DE            Short=dSiR alpha {ECO:0000303|PubMed:18829451};
DE   AltName: Full=Hydrogensulfite reductase subunit alpha;
GN   Name=dsvA; Synonyms=dsrA {ECO:0000303|PubMed:18829451};
GN   OrderedLocusNames=DVU_0402;
OS   Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 /
OS   NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris).
OC   Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia;
OC   Desulfovibrionales; Desulfovibrionaceae; Nitratidesulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7887608; DOI=10.1128/aem.61.1.290-296.1995;
RA   Karkhoff-Schweizer R.R., Huber D.P.W., Voordouw G.;
RT   "Conservation of the genes for dissimilatory sulfite reductase from
RT   Desulfovibrio vulgaris and Archaeoglobus fulgidus allows their detection by
RT   PCR.";
RL   Appl. Environ. Microbiol. 61:290-296(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 /
RC   Hildenborough;
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA   Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA   Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA   Wall J.D., Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-26, AND SUBUNIT.
RX   PubMed=1555572; DOI=10.1111/j.1432-1033.1992.tb16757.x;
RA   Pierik A.J., Duyvis M.G., van Helvoort J.M.L.M., Wolbert R.B.G.,
RA   Hagen W.R.;
RT   "The third subunit of desulfoviridin-type dissimilatory sulfite
RT   reductases.";
RL   Eur. J. Biochem. 205:111-115(1992).
RN   [4]
RP   CHARACTERIZATION.
RX   PubMed=4725615; DOI=10.1128/jb.115.2.529-542.1973;
RA   Lee J.-P., LeGall J., Peck H.D. Jr.;
RT   "Isolation of assimilatory- and dissimilatory-type sulfite reductases from
RT   Desulfovibrio vulgaris.";
RL   J. Bacteriol. 115:529-542(1973).
RN   [5]
RP   FUNCTION, AND EPR SPECTROSCOPY.
RX   PubMed=8033912; DOI=10.1111/j.1432-1033.1994.tb18968.x;
RA   Wolfe B.M., Lui S.M., Cowan J.A.;
RT   "Desulfoviridin, a multimeric-dissimilatory sulfite reductase from
RT   Desulfovibrio vulgaris (Hildenborough). Purification, characterization,
RT   kinetics and EPR studies.";
RL   Eur. J. Biochem. 223:79-89(1994).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH DSVB; DSVC;
RP   SIROHYDROCHLORIN AND IRON-SULFUR (4FE-4S), AND SUBUNIT.
RX   PubMed=18829451; DOI=10.1074/jbc.m805643200;
RA   Oliveira T.F., Vonrhein C., Matias P.M., Venceslau S.S., Pereira I.A.C.,
RA   Archer M.;
RT   "The crystal structure of Desulfovibrio vulgaris dissimilatory sulfite
RT   reductase bound to DsrC provides novel insights into the mechanism of
RT   sulfate respiration.";
RL   J. Biol. Chem. 283:34141-34149(2008).
CC   -!- FUNCTION: Part of the complex that catalyzes the reduction of sulfite
CC       to sulfide. The alpha and beta subunits may have arisen by gene
CC       duplication. They both bind 2 iron-sulfur clusters, but the alpha
CC       subunit seems to be catalytically inactive, due to substitutions along
CC       the putative substrate access channel, and because it binds
CC       sirohydrochlorin (the dematallated form of siroheme) instead of
CC       siroheme. {ECO:0000269|PubMed:1555572, ECO:0000269|PubMed:8033912}.
CC   -!- SUBUNIT: Heterohexamer of two alpha, two beta and two gamma subunits.
CC       {ECO:0000269|PubMed:1555572, ECO:0000269|PubMed:18829451}.
CC   -!- INTERACTION:
CC       P45574; P45575: dsvB; NbExp=5; IntAct=EBI-9016991, EBI-9016987;
CC       P45574; P45573: dsvC; NbExp=3; IntAct=EBI-9016991, EBI-9017020;
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DR   EMBL; U16723; AAA70107.1; -; Genomic_DNA.
DR   EMBL; AE017285; AAS94885.1; -; Genomic_DNA.
DR   PIR; S21197; S21197.
DR   RefSeq; WP_010937709.1; NC_002937.3.
DR   PDB; 2V4J; X-ray; 2.10 A; A/D=1-437.
DR   AlphaFoldDB; P45574; -.
DR   SMR; P45574; -.
DR   IntAct; P45574; 6.
DR   STRING; 882.DVU_0402; -.
DR   PaxDb; 882-DVU_0402; -.
DR   EnsemblBacteria; AAS94885; AAS94885; DVU_0402.
DR   KEGG; dvu:DVU_0402; -.
DR   PATRIC; fig|882.5.peg.379; -.
DR   eggNOG; COG2221; Bacteria.
DR   HOGENOM; CLU_660112_0_0_7; -.
DR   OrthoDB; 9800558at2; -.
DR   PhylomeDB; P45574; -.
DR   BioCyc; MetaCyc:MONOMER-12511; -.
DR   BRENDA; 1.8.1.22; 1914.
DR   EvolutionaryTrace; P45574; -.
DR   Proteomes; UP000002194; Chromosome.
DR   GO; GO:0009337; C:sulfite reductase complex (NADPH); IEA:TreeGrafter.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0018551; F:dissimilatory sulfite reductase (NADH) activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0050311; F:sulfite reductase (ferredoxin) activity; IEA:TreeGrafter.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:TreeGrafter.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.30.70.2500; -; 1.
DR   Gene3D; 6.10.140.1420; -; 1.
DR   Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR011806; DsrA.
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   NCBIfam; TIGR02064; dsrA; 1.
DR   PANTHER; PTHR11493:SF54; ANAEROBIC SULFITE REDUCTASE SUBUNIT C; 1.
DR   PANTHER; PTHR11493; SULFITE REDUCTASE [NADPH] SUBUNIT BETA-RELATED; 1.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 1.
DR   SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
DR   PDBsum; 2V4J; -.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur;
KW   Metal-binding; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1555572"
FT   CHAIN           2..437
FT                   /note="Sulfite reductase, dissimilatory-type subunit alpha"
FT                   /id="PRO_0000080030"
FT   DOMAIN          294..322
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         177
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:18829451,
FT                   ECO:0007744|PDB:2V4J"
FT   BINDING         183
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:18829451,
FT                   ECO:0007744|PDB:2V4J"
FT   BINDING         221
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:18829451,
FT                   ECO:0007744|PDB:2V4J"
FT   BINDING         225
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:18829451,
FT                   ECO:0007744|PDB:2V4J"
FT   BINDING         284
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:18829451,
FT                   ECO:0007744|PDB:2V4J"
FT   BINDING         303
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:18829451,
FT                   ECO:0007744|PDB:2V4J"
FT   BINDING         306
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:18829451,
FT                   ECO:0007744|PDB:2V4J"
FT   BINDING         309
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:18829451,
FT                   ECO:0007744|PDB:2V4J"
FT   CONFLICT        22
FT                   /note="S -> V (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        26
FT                   /note="Q -> K (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           9..13
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          14..17
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           20..33
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           46..60
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          79..81
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          84..87
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   TURN            88..90
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           92..94
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          99..102
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          109..111
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           112..125
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          128..132
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          139..142
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           146..158
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          168..171
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           172..174
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           179..181
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           190..200
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           202..206
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          210..212
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          216..221
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           228..231
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          233..242
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           248..255
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           261..264
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   TURN            265..268
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           276..279
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           281..283
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          289..291
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          296..298
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           300..302
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           308..312
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   TURN            314..316
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          321..329
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   TURN            335..337
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          343..349
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           356..372
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           379..386
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           388..394
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           401..403
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   STRAND          404..406
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           417..419
FT                   /evidence="ECO:0007829|PDB:2V4J"
FT   HELIX           428..434
FT                   /evidence="ECO:0007829|PDB:2V4J"
SQ   SEQUENCE   437 AA;  49091 MW;  4AED624D4B13A21F CRC64;
     MAKHATPKLD QLESGPWPSF VSDIKQEAAY RAANPKGLDY QVPVDCPEDL LGVLELSYDE
     GETHWKHGGI VGVFGYGGGV IGRYCDQPEK FPGVAHFHTV RVAQPSGKYY SADYLRQLCD
     IWDLRGSGLT NMHGSTGDIV LLGTQTPQLE EIFFELTHNL NTDLGGSGSN LRTPESCLGK
     SRCEFACYDS QAACYELTME YQDELHRPAF PYKFKFKFDA CPNGCVASIA RSDFSVIGTW
     KDDIKIDAEA VKAYVAGEFK PNAGAHSGRD WGKFDIEAEV VNRCPSKCMK WDGSKLSIDN
     KECVRCMHCI NTMPRALHIG DERGASILCG AKAPILDGAQ MGSLLVPFVA AEEPFDEIKE
     VVEKIWDWWM EEGKNRERLG ETMKRLSFQK LLEVTEIAPV PQHVKEPRTN PYIFFKEEEV
     PGGWDRDITE YRKRHLR
//