PHSS_DESBA
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 03-AUG-2022, entry version 131.
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; DOI=10.1128/jb.169.12.5401-5407.1987;
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 subunits
RT of the periplasmic (NiFeSe) hydrogenase of Desulfovibrio baculatus.";
RL J. Bacteriol. 169:5401-5407(1987).
RN [2]
RP ERRATUM OF PUBMED:3316183, 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 image
RT of the activated catalytic center.";
RL Structure 7:557-566(1999).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + H2 = AH2; Xref=Rhea:RHEA:12116, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:18276; EC=1.12.99.6;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 3 [4Fe-4S] clusters. Cluster 1 is referred to as proximal,
CC 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 the
CC signal peptide cleavage has been experimentally proven.
CC -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit
CC 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 AlphaFoldDB; P13063; -.
DR SMR; P13063; -.
DR DIP; DIP-6126N; -.
DR IntAct; P13063; 1.
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: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; IPR037148; NiFe-Hase_small_C_sf.
DR InterPro; IPR037024; NiFe_Hase_small_N_sf.
DR InterPro; IPR001821; NiFe_hydrogenase_ssu.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR PANTHER; PTHR30013; PTHR30013; 1.
DR Pfam; PF14720; NiFe_hyd_SSU_C; 1.
DR Pfam; PF01058; Oxidored_q6; 1.
DR PIRSF; PIRSF000310; NiFe_hyd_ssu; 1.
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
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:3322275"
FT CHAIN 33..315
FT /note="Periplasmic [NiFeSe] hydrogenase small subunit"
FT /id="PRO_0000013420"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT BINDING 158
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT BINDING 196
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT BINDING 240
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT BINDING 243
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT BINDING 263
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT BINDING 269
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT BINDING 278
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT BINDING 290
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT BINDING 296
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT BINDING 299
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:4KN9"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:4KN9"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:4KN9"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:4KN9"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:4KN9"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:4KN9"
FT HELIX 86..99
FT /evidence="ECO:0007829|PDB:4KN9"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:4KN9"
FT STRAND 103..113
FT /evidence="ECO:0007829|PDB:4KN9"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:4KN9"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:4KN9"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:4KL8"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:4KN9"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:4KN9"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:4KN9"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:4KN9"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:4KN9"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:4KN9"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:4KN9"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:4KN9"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:4KN9"
FT HELIX 200..215
FT /evidence="ECO:0007829|PDB:4KN9"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:4KN9"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:4KN9"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:4KN9"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:4KN9"
FT HELIX 246..250
FT /evidence="ECO:0007829|PDB:4KN9"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:4KN9"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:4KN9"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:4KN9"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:4KN9"
FT TURN 284..287
FT /evidence="ECO:0007829|PDB:4KN9"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:4KN9"
FT TURN 302..305
FT /evidence="ECO:0007829|PDB:4KN9"
FT HELIX 306..308
FT /evidence="ECO:0007829|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
