DSVA_DESVH
ID DSVA_DESVH Reviewed; 437 AA.
AC P45574; Q46581;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 131.
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 Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
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 / NCIMB 8303 / VKM B-1760 / 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; NZ_CABHLV010000001.1.
DR RefSeq; YP_009626.1; NC_002937.3.
DR PDB; 2V4J; X-ray; 2.10 A; A/D=1-437.
DR PDBsum; 2V4J; -.
DR AlphaFoldDB; P45574; -.
DR SMR; P45574; -.
DR IntAct; P45574; 6.
DR STRING; 882.DVU_0402; -.
DR PaxDb; P45574; -.
DR PRIDE; P45574; -.
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 OMA; MHCLNVM; -.
DR PhylomeDB; P45574; -.
DR BioCyc; MetaCyc:MON-12511; -.
DR BRENDA; 1.8.99.5; 1914.
DR EvolutionaryTrace; P45574; -.
DR Proteomes; UP000002194; Chromosome.
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; 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..148
FT /evidence="ECO:0007829|PDB:2V4J"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:2V4J"
FT STRAND 168..171
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
