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   16-JUN-2009, entry version 81.
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 Hildenborough / ATCC 29579 / NCIMB
OS   8303).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=85203856; PubMed=3888621;
RX   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].
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.,
RA   Dimitrov G., Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R.,
RA   Feldblyum T.V., 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   MEDLINE=88106446; 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   MEDLINE=86277938; PubMed=3525521;
RA   Prickril B.C., Czechowski M.H., Przybyla A.E., Peck H.D. Jr.,
RA   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   MEDLINE=99148109; PubMed=10368269; DOI=10.1016/S0969-2126(99)80005-7;
RA   Nicolet Y., Piras C., Legrand P., Hatchikian E.C.,
RA   Fontecilla-Camps J.-C.;
RT   "Desulfovibrio desulfuricans iron hydrogenase: the structure shows
RT   unusual 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.
CC       Cytochrome c3 is likely to be the physiological electron carrier
CC       for the enzyme.
CC   -!- CATALYTIC ACTIVITY: H(2) + 2 oxidized ferredoxin = 2 reduced
CC       ferredoxin + 2 H(+).
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
CC       the 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; YP_010988.1; -.
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   PDBsum; 1E08; -.
DR   PDBsum; 1GX7; -.
DR   PDBsum; 1HFE; -.
DR   DIP; DIP:6187N; -.
DR   GeneID; 2795817; -.
DR   GenomeReviews; AE017285_GR; DVU_1770.
DR   KEGG; dvu:DVU1770; -.
DR   TIGR; DVU_1770; -.
DR   HOGENOM; P07603; -.
DR   OMA; P07603; VSHANPA.
DR   BioCyc; DVUL882:DVU_1770-MON; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR003149; Fe_hydrogenase_ssu-like.
DR   InterPro; IPR006311; Tat.
DR   InterPro; IPR017909; Twin_arg_translocation_Tat.
DR   Gene3D; G3DSA:4.10.260.20; Fe_hyd_ssu-like; 1.
DR   Pfam; PF02256; Fe_hyd_SSU; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Direct protein sequencing; Iron;
KW   Iron-sulfur; Metal-binding; Oxidoreductase; Periplasm; Signal.
FT   SIGNAL        1     34       Tat-type signal.
FT   CHAIN        35    123       Periplasmic [Fe] hydrogenase small
FT                                subunit.
FT                                /FTId=PRO_0000013413.
FT   HELIX        39     56
FT   HELIX        62     64
FT   HELIX        66     74
FT   HELIX        82     88
FT   HELIX        97    104
FT   HELIX       113    116
SQ   SEQUENCE   123 AA;  13624 MW;  2F4F7A4304ECD47B CRC64;
     MQIASITRRG FLKVACVTTG AALIGIRMTG KAVAAVKQIK DYMLDRINGV YGADAKFPVR
     ASQDNTQVKA LYKSYLEKPL GHKSHDLLHT HWFDKSKGVK ELTTAGKLPN PRASEFEGPY
     PYE
//