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-MAY-2013, entry version 95.
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 Desulfovibrio baculatus (Desulfomicrobium 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.
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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 PDBsum; 1CC1; -.
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-SubCell.
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:EC.
DR GO; GO:0046872; F:metal 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 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; 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.
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 121 124
FT STRAND 131 133
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 HELIX 200 215
FT TURN 217 219
FT HELIX 232 235
FT STRAND 236 238
FT TURN 239 242
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
//
