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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   29-OCT-2014, entry version 102.
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: 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
FT   HELIX        52     58
FT   TURN         61     64
FT   HELIX        65     71
FT   STRAND       73     77
FT   TURN         79     81
FT   HELIX        86     99
FT   TURN        100    102
FT   STRAND      103    113
FT   HELIX       115    118
FT   STRAND      121    127
FT   STRAND      129    131
FT   STRAND      133    137
FT   HELIX       138    145
FT   HELIX       146    148
FT   STRAND      149    156
FT   HELIX       157    161
FT   HELIX       164    166
FT   HELIX       177    184
FT   STRAND      190    193
FT   STRAND      195    197
FT   HELIX       200    215
FT   TURN        217    219
FT   HELIX       232    235
FT   STRAND      236    238
FT   HELIX       240    242
FT   HELIX       246    250
FT   STRAND      260    264
FT   HELIX       265    267
FT   HELIX       271    273
FT   HELIX       278    281
FT   TURN        284    287
FT   HELIX       290    293
FT   TURN        302    305
FT   HELIX       306    308
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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