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Database: UniProt
Entry: P13063
LinkDB: P13063
Original site: P13063 
ID   PHSS_DESBA              Reviewed;         315 AA.
AC   P13063;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   26-NOV-2014, entry version 103.
DE   RecName: Full=Periplasmic [NiFeSe] hydrogenase small subunit;
DE            EC=1.12.99.6;
DE   AltName: Full=NiFeSe hydrogenlyase small chain;
DE   Flags: Precursor;
OS   Desulfomicrobium baculatum (Desulfovibrio baculatus).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfomicrobiaceae; Desulfomicrobium.
OX   NCBI_TaxID=899;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3316183;
RA   Menon N.K., Peck H.D. Jr., le Gall J., Przybyla A.E.;
RT   "Cloning and sequencing of the genes encoding the large and small
RT   subunits of the periplasmic (NiFeSe) hydrogenase of Desulfovibrio
RT   baculatus.";
RL   J. Bacteriol. 169:5401-5407(1987).
RN   [2]
RP   ERRATUM, AND SEQUENCE REVISION.
RA   Menon N.K., Pect H.D. Jr., le Gall J., Przybyla A.E.;
RL   J. Bacteriol. 170:4429-4429(1988).
RN   [3]
RP   PROTEIN SEQUENCE OF 33-67.
RC   STRAIN=DSM 1743;
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   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
RX   PubMed=10378275; DOI=10.1016/S0969-2126(99)80072-0;
RA   Garcin E., Vernede X., Hatchikian E.C., Volbeda A., Frey M.,
RA   Fontecilla-Camps J.-C.;
RT   "The crystal structure of a reduced [NiFeSe] hydrogenase provides an
RT   image of the activated catalytic center.";
RL   Structure 7:557-566(1999).
CC   -!- CATALYTIC ACTIVITY: H(2) + A = AH(2).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 3 [4Fe-4S] clusters. Cluster 1 is referred to as
CC       proximal, cluster 2 as distal, cluster 3 as medial.;
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.
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase small
CC       subunit family. {ECO:0000305}.
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DR   EMBL; M18271; AAA23376.1; -; Genomic_DNA.
DR   PIR; A28380; HQDVSB.
DR   PDB; 1CC1; X-ray; 2.15 A; S=33-315.
DR   PDB; 4KL8; X-ray; 1.52 A; S/T=33-315.
DR   PDB; 4KN9; X-ray; 1.40 A; S/T=33-315.
DR   PDB; 4KO1; X-ray; 1.55 A; S/T=33-315.
DR   PDB; 4KO2; X-ray; 1.60 A; S/T=33-315.
DR   PDB; 4KO3; X-ray; 1.70 A; S/T=33-315.
DR   PDB; 4KO4; X-ray; 2.00 A; S/T=33-315.
DR   PDBsum; 1CC1; -.
DR   PDBsum; 4KL8; -.
DR   PDBsum; 4KN9; -.
DR   PDBsum; 4KO1; -.
DR   PDBsum; 4KO2; -.
DR   PDBsum; 4KO3; -.
DR   PDBsum; 4KO4; -.
DR   ProteinModelPortal; P13063; -.
DR   SMR; P13063; 38-315.
DR   DIP; DIP-6126N; -.
DR   MINT; MINT-96877; -.
DR   EvolutionaryTrace; P13063; -.
DR   GO; GO:0009375; C:ferredoxin hydrogenase complex; IEA:InterPro.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR   GO; GO:0033748; F:hydrogenase (acceptor) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.700; -; 1.
DR   Gene3D; 4.10.480.10; -; 1.
DR   InterPro; IPR027394; Cytochrome-c3_hydrogenase_C.
DR   InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR   InterPro; IPR001821; NiFe_hydrogenase_ssu.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   Pfam; PF14720; NiFe_hyd_SSU_C; 1.
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   3D-structure; 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur;
KW   Metal-binding; Oxidoreductase; Periplasm; Signal.
FT   SIGNAL        1     32       Tat-type signal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00648,
FT                                ECO:0000269|PubMed:3322275}.
FT   CHAIN        33    315       Periplasmic [NiFeSe] hydrogenase small
FT                                subunit.
FT                                /FTId=PRO_0000013420.
FT   METAL        50     50       Iron-sulfur 1 (4Fe-4S).
FT   METAL        53     53       Iron-sulfur 1 (4Fe-4S).
FT   METAL       158    158       Iron-sulfur 1 (4Fe-4S).
FT   METAL       196    196       Iron-sulfur 1 (4Fe-4S).
FT   METAL       240    240       Iron-sulfur 2 (4Fe-4S); via pros
FT                                nitrogen.
FT   METAL       243    243       Iron-sulfur 2 (4Fe-4S).
FT   METAL       263    263       Iron-sulfur 2 (4Fe-4S).
FT   METAL       269    269       Iron-sulfur 2 (4Fe-4S).
FT   METAL       278    278       Iron-sulfur 3 (4Fe-4S).
FT   METAL       290    290       Iron-sulfur 3 (4Fe-4S).
FT   METAL       296    296       Iron-sulfur 3 (4Fe-4S).
FT   METAL       299    299       Iron-sulfur 3 (4Fe-4S).
FT   STRAND       40     48       {ECO:0000244|PDB:4KN9}.
FT   HELIX        52     58       {ECO:0000244|PDB:4KN9}.
FT   TURN         61     64       {ECO:0000244|PDB:4KN9}.
FT   HELIX        65     71       {ECO:0000244|PDB:4KN9}.
FT   STRAND       73     77       {ECO:0000244|PDB:4KN9}.
FT   TURN         79     81       {ECO:0000244|PDB:4KN9}.
FT   HELIX        86     99       {ECO:0000244|PDB:4KN9}.
FT   TURN        100    102       {ECO:0000244|PDB:4KN9}.
FT   STRAND      103    113       {ECO:0000244|PDB:4KN9}.
FT   HELIX       115    118       {ECO:0000244|PDB:4KN9}.
FT   STRAND      121    127       {ECO:0000244|PDB:4KN9}.
FT   STRAND      129    131       {ECO:0000244|PDB:4KL8}.
FT   STRAND      133    137       {ECO:0000244|PDB:4KN9}.
FT   HELIX       138    145       {ECO:0000244|PDB:4KN9}.
FT   HELIX       146    148       {ECO:0000244|PDB:4KN9}.
FT   STRAND      149    156       {ECO:0000244|PDB:4KN9}.
FT   HELIX       157    161       {ECO:0000244|PDB:4KN9}.
FT   HELIX       164    166       {ECO:0000244|PDB:4KN9}.
FT   HELIX       177    184       {ECO:0000244|PDB:4KN9}.
FT   STRAND      190    193       {ECO:0000244|PDB:4KN9}.
FT   STRAND      195    197       {ECO:0000244|PDB:4KN9}.
FT   HELIX       200    215       {ECO:0000244|PDB:4KN9}.
FT   TURN        217    219       {ECO:0000244|PDB:4KN9}.
FT   HELIX       232    235       {ECO:0000244|PDB:4KN9}.
FT   STRAND      236    238       {ECO:0000244|PDB:4KN9}.
FT   HELIX       240    242       {ECO:0000244|PDB:4KN9}.
FT   HELIX       246    250       {ECO:0000244|PDB:4KN9}.
FT   STRAND      260    264       {ECO:0000244|PDB:4KN9}.
FT   HELIX       265    267       {ECO:0000244|PDB:4KN9}.
FT   HELIX       271    273       {ECO:0000244|PDB:4KN9}.
FT   HELIX       278    281       {ECO:0000244|PDB:4KN9}.
FT   TURN        284    287       {ECO:0000244|PDB:4KN9}.
FT   HELIX       290    293       {ECO:0000244|PDB:4KN9}.
FT   TURN        302    305       {ECO:0000244|PDB:4KN9}.
FT   HELIX       306    308       {ECO:0000244|PDB:4KN9}.
SQ   SEQUENCE   315 AA;  34221 MW;  A3C592F12B95ED83 CRC64;
     MSLSRREFVK LCSAGVAGLG ISQIYHPGIV HAMTEGAKKA PVIWVQGQGC TGCSVSLLNA
     VHPRIKEILL DVISLEFHPT VMASEGEMAL AHMYEIAEKF NGNFFLLVEG AIPTAKEGRY
     CIVGETLDAK GHHHEVTMME LIRDLAPKSL ATVAVGTCSA YGGIPAAEGN VTGSKSVRDF
     FADEKIEKLL VNVPGCPPHP DWMVGTLVAA WSHVLNPTEH PLPELDDDGR PLLFFGDNIH
     ENCPYLDKYD NSEFAETFTK PGCKAELGCK GPSTYADCAK RRWNNGINWC VENAVCIGCV
     EPDFPDGKSP FYVAE
//
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