ID   PHNS1_DESVH             Reviewed;         317 AA.
AC   Q06173;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   16-JUN-2009, entry version 69.
DE   RecName: Full=Periplasmic [NiFe] hydrogenase small subunit 1;
DE            EC=1.12.2.1;
DE   AltName: Full=NiFe hydrogenlyase small chain 1;
DE   Flags: Precursor;
GN   Name=hynB1; Synonyms=hynB-1; OrderedLocusNames=DVU_1921;
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 [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   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55, AND MUTAGENESIS OF ARG-18.
RX   MEDLINE=93123973; PubMed=1479348;
RA   Niviere V., Wong S.L., Voordouw G.;
RT   "Site-directed mutagenesis of the hydrogenase signal peptide consensus
RT   box prevents export of a beta-lactamase fusion protein.";
RL   J. Gen. Microbiol. 138:2173-2183(1992).
CC   -!- CATALYTIC ACTIVITY: 2 H(2) + ferricytochrome c3 = 4 H(+) +
CC       ferrocytochrome c3.
CC   -!- COFACTOR: Binds 1 3Fe-4S cluster (By similarity).
CC   -!- COFACTOR: Binds 2 4Fe-4S clusters (By similarity).
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 not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase small
CC       subunit family.
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DR   EMBL; AE017285; AAS96397.1; -; Genomic_DNA.
DR   RefSeq; YP_011138.1; -.
DR   SMR; Q06173; 51-317.
DR   GeneID; 2793337; -.
DR   GenomeReviews; AE017285_GR; DVU_1921.
DR   KEGG; dvu:DVU1921; -.
DR   TIGR; DVU_1921; -.
DR   HOGENOM; Q06173; -.
DR   OMA; Q06173; RLIHENC.
DR   BioCyc; DVUL882:DVU_1921-MON; -.
DR   GO; GO:0009375; C:ferredoxin hydrogenase complex; IEA:InterPro.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0047806; F:cytochrome-c3 hydrogenase activity; IEA:EC.
DR   GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR   InterPro; IPR001821; NiFe_hydrogenase_ssu.
DR   InterPro; IPR006311; Tat.
DR   InterPro; IPR017909; Twin_arg_translocation_Tat.
DR   Pfam; PF01058; Oxidored_q6; 1.
DR   PIRSF; PIRSF000310; NiFe_hyd_ssu; 1.
DR   PRINTS; PR00614; NIHGNASESMLL.
DR   TIGRFAMs; TIGR00391; hydA; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   3Fe-4S; 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding;
KW   Oxidoreductase; Periplasm; Signal.
FT   SIGNAL        1     49       Tat-type signal (Potential).
FT   CHAIN        50    317       Periplasmic [NiFe] hydrogenase small
FT                                subunit 1.
FT                                /FTId=PRO_0000013417.
FT   METAL        67     67       Iron-sulfur 1 (4Fe-4S) (By similarity).
FT   METAL        70     70       Iron-sulfur 1 (4Fe-4S) (By similarity).
FT   METAL       164    164       Iron-sulfur 1 (4Fe-4S) (By similarity).
FT   METAL       200    200       Iron-sulfur 1 (4Fe-4S) (By similarity).
FT   METAL       238    238       Iron-sulfur 2 (4Fe-4S); via pros nitrogen
FT                                (By similarity).
FT   METAL       241    241       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       266    266       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       272    272       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       281    281       Iron-sulfur 3 (3Fe-4S) (By similarity).
FT   METAL       299    299       Iron-sulfur 3 (3Fe-4S) (By similarity).
FT   METAL       302    302       Iron-sulfur 3 (3Fe-4S) (By similarity).
FT   MUTAGEN      18     18       R->E: Completely inhibits export and
FT                                processing of the fusion protein.
SQ   SEQUENCE   317 AA;  34236 MW;  E579C0215F1C5F47 CRC64;
     MRFSVGLGKE GAEERLARRG VSRRDFLKFC TAIAVTMGMG PAFAPEVARA LTGSRRPSVV
     YLHNAECTGC SESVLRAFQP YLDELILDTI SLDYHETIMA AAGDAAEAAL HQAVANPDGF
     ICIVEGAIPT ADNGIYGKVA NHTMLSICSD IVPKAKAVIA YGTCATFGGV QAAKPNPTGA
     KGLNDALKHL GVNAINLAGC PPNPYNLVGT LVYYLKNNAA PEMDEFNRPL MFFGQSVHDN
     CPRLKHFDAG EFAPSFESEE ARKGWCLYEL GCKGPSTMNN CPKIKFNQTN WPVEAGHPCI
     GCSEPDFWDE KSPFYES
//