ID   PHFS_DESVH              Reviewed;         123 AA.
AC   P07603;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=Periplasmic [Fe] hydrogenase small subunit;
DE            EC=1.12.7.2;
DE   AltName: Full=Fe hydrogenlyase small chain;
DE   Flags: Precursor;
GN   Name=hydB; OrderedLocusNames=DVU_1770;
OS   Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS   B-1760 / Hildenborough).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Nitratidesulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3888621; DOI=10.1111/j.1432-1033.1985.tb08869.x;
RA   Voordouw G., Brenner S.;
RT   "Nucleotide sequence of the gene encoding the hydrogenase from
RT   Desulfovibrio vulgaris (Hildenborough).";
RL   Eur. J. Biochem. 148:515-520(1985).
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 35-69.
RX   PubMed=3322275; DOI=10.1016/0006-291x(87)90376-7;
RA   Prickril B.C., He S.H., Li C., Menon N.K., Choi E.S., Przybyla A.E.,
RA   Dervartanian D.V., Peck H.D. Jr., Fauque G., le Gall J., Teixeira M.,
RA   Moura I., Moura J.J.G., Patil D., Huynh B.H.;
RT   "Identification of three classes of hydrogenase in the genus,
RT   Desulfovibrio.";
RL   Biochem. Biophys. Res. Commun. 149:369-377(1987).
RN   [4]
RP   SIGNAL SEQUENCE CLEAVAGE SITE.
RX   PubMed=3525521; DOI=10.1128/jb.167.2.722-725.1986;
RA   Prickril B.C., Czechowski M.H., Przybyla A.E., Peck H.D. Jr., le Gall J.;
RT   "Putative signal peptide on the small subunit of the periplasmic
RT   hydrogenase from Desulfovibrio vulgaris.";
RL   J. Bacteriol. 167:722-725(1986).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX   PubMed=10368269; DOI=10.1016/s0969-2126(99)80005-7;
RA   Nicolet Y., Piras C., Legrand P., Hatchikian E.C., Fontecilla-Camps J.-C.;
RT   "Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual
RT   coordination to an active site Fe binuclear center.";
RL   Structure 7:13-23(1999).
CC   -!- FUNCTION: May be involved in hydrogen uptake for the reduction of
CC       sulfate to hydrogen sulfide in an electron transport chain. Cytochrome
CC       c3 is likely to be the physiological electron carrier for the enzyme.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2 + 2 oxidized [2Fe-2S]-[ferredoxin] = 2 H(+) + 2 reduced
CC         [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:17445, Rhea:RHEA-COMP:10000,
CC         Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:18276,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.12.7.2;
CC   -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has been experimentally proven.
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DR   EMBL; X02416; CAA26267.1; -; Genomic_DNA.
DR   EMBL; AE017285; AAS96247.1; -; Genomic_DNA.
DR   PIR; B24551; HQDVFS.
DR   RefSeq; WP_010939058.1; NZ_CABHLV010000001.1.
DR   RefSeq; YP_010988.1; NC_002937.3.
DR   PDB; 1E08; NMR; -; D=36-123.
DR   PDB; 1GX7; NMR; -; D=36-123.
DR   PDB; 1HFE; X-ray; 1.60 A; S/T=1-123.
DR   PDB; 8BJ7; X-ray; 1.04 A; B=36-123.
DR   PDB; 8BJ8; X-ray; 1.01 A; B=36-123.
DR   PDBsum; 1E08; -.
DR   PDBsum; 1GX7; -.
DR   PDBsum; 1HFE; -.
DR   PDBsum; 8BJ7; -.
DR   PDBsum; 8BJ8; -.
DR   AlphaFoldDB; P07603; -.
DR   SMR; P07603; -.
DR   DIP; DIP-6187N; -.
DR   IntAct; P07603; 1.
DR   STRING; 882.DVU_1770; -.
DR   PaxDb; 882-DVU_1770; -.
DR   EnsemblBacteria; AAS96247; AAS96247; DVU_1770.
DR   KEGG; dvu:DVU_1770; -.
DR   PATRIC; fig|882.5.peg.1626; -.
DR   eggNOG; COG4624; Bacteria.
DR   HOGENOM; CLU_163904_0_0_7; -.
DR   OrthoDB; 5460598at2; -.
DR   BioCyc; MetaCyc:MONOMER-22145; -.
DR   EvolutionaryTrace; P07603; -.
DR   Proteomes; UP000002194; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.260.20; Iron hydrogenase, small subunit; 1.
DR   InterPro; IPR008953; Fe_hydrogenase_HydB.
DR   InterPro; IPR003149; Fe_hydrogenase_ssu.
DR   InterPro; IPR036991; Fe_hydrogenase_ssu_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR   Pfam; PF02256; Fe_hyd_SSU; 1.
DR   SMART; SM00902; Fe_hyd_SSU; 1.
DR   SUPFAM; SSF48674; Fe-only hydrogenase smaller subunit; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW   Oxidoreductase; Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..34
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT                   ECO:0000269|PubMed:3322275, ECO:0000269|PubMed:3525521"
FT   CHAIN           35..123
FT                   /note="Periplasmic [Fe] hydrogenase small subunit"
FT                   /id="PRO_0000013413"
FT   REGION          103..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           39..55
FT                   /evidence="ECO:0007829|PDB:8BJ7"
FT   HELIX           62..64
FT                   /evidence="ECO:0007829|PDB:8BJ7"
FT   HELIX           66..74
FT                   /evidence="ECO:0007829|PDB:8BJ7"
FT   HELIX           82..88
FT                   /evidence="ECO:0007829|PDB:8BJ7"
FT   HELIX           97..104
FT                   /evidence="ECO:0007829|PDB:8BJ7"
FT   HELIX           113..116
FT                   /evidence="ECO:0007829|PDB:8BJ7"
SQ   SEQUENCE   123 AA;  13624 MW;  2F4F7A4304ECD47B CRC64;
     MQIASITRRG FLKVACVTTG AALIGIRMTG KAVAAVKQIK DYMLDRINGV YGADAKFPVR
     ASQDNTQVKA LYKSYLEKPL GHKSHDLLHT HWFDKSKGVK ELTTAGKLPN PRASEFEGPY
     PYE
//