PHFS_DESVH
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 03-AUG-2022, entry version 145.
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; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 PDBsum; 1E08; -.
DR PDBsum; 1GX7; -.
DR PDBsum; 1HFE; -.
DR AlphaFoldDB; P07603; -.
DR SMR; P07603; -.
DR DIP; DIP-6187N; -.
DR IntAct; P07603; 1.
DR STRING; 882.DVU_1770; -.
DR PaxDb; P07603; -.
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 OMA; PAVEKYY; -.
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; -; 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 Pfam; PF02256; Fe_hyd_SSU; 1.
DR SMART; SM00902; Fe_hyd_SSU; 1.
DR SUPFAM; SSF48674; SSF48674; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 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..56
FT /evidence="ECO:0007829|PDB:1HFE"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1HFE"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:1HFE"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:1HFE"
FT HELIX 97..104
FT /evidence="ECO:0007829|PDB:1HFE"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:1HFE"
SQ SEQUENCE 123 AA; 13624 MW; 2F4F7A4304ECD47B CRC64;
MQIASITRRG FLKVACVTTG AALIGIRMTG KAVAAVKQIK DYMLDRINGV YGADAKFPVR
ASQDNTQVKA LYKSYLEKPL GHKSHDLLHT HWFDKSKGVK ELTTAGKLPN PRASEFEGPY
PYE
