ID PHNS_SOLFR Reviewed; 314 AA. AC P18187; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 4. DT 02-SEP-2026, entry version 162. DE RecName: Full=Periplasmic [NiFe] hydrogenase small subunit; DE EC=1.12.2.1; DE AltName: Full=NiFe hydrogenlyase small chain; DE Flags: Precursor; GN Name=hydA; OS Solidesulfovibrio fructosivorans (Desulfovibrio fructosivorans). OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia; OC Desulfovibrionales; Desulfovibrionaceae; Solidesulfovibrio. OX NCBI_TaxID=878; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 49200 / DSM 3604 / VKM B-1801 / JJ; RX PubMed=2227457; DOI=10.1016/0378-1119(90)90473-5; RA Rousset M., Dermoun Z., Matchikian C.E., Belaich J.-P.; RT "Cloning and sequencing of the locus encoding the large and small subunit RT genes of the periplasmic [NiFe]hydrogenase from Desulfovibrio RT fructosovorans."; RL Gene 94:95-101(1990). RN [2] RP PROTEIN SEQUENCE OF 50-60. RX PubMed=2154378; DOI=10.1111/j.1432-1033.1990.tb15347.x; RA Hatchikian C.E., Traore A.S., Fernandez V.M., Cammack R.; RT "Characterization of the nickel-iron periplasmic hydrogenase from RT Desulfovibrio fructosovorans."; RL Eur. J. Biochem. 187:635-643(1990). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 51-314 IN COMPLEX WITH HYDB AND RP IRON-SULFUR CLUSTERS, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF RP PRO-238. RX PubMed=9751716; DOI=10.1073/pnas.95.20.11625; RA Rousset M., Montet Y., Guigliarelli B., Forget N., Asso M., Bertrand P., RA Fontecilla-Camps J.C., Hatchikian E.C.; RT "[3Fe-4S] to [4Fe-4S] cluster conversion in Desulfovibrio fructosovorans RT [NiFe] hydrogenase by site-directed mutagenesis."; RL Proc. Natl. Acad. Sci. U.S.A. 95:11625-11630(1998). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 51-314 IN COMPLEX WITH HYDB AND RP IRON-SULFUR CLUSTERS. RX PubMed=15803334; DOI=10.1007/s00775-005-0632-x; RA Volbeda A., Martin L., Cavazza C., Matho M., Faber B.W., Roseboom W., RA Albracht S.P., Garcin E., Rousset M., Fontecilla-Camps J.C.; RT "Structural differences between the ready and unready oxidized states of RT [NiFe] hydrogenases."; RL J. Biol. Inorg. Chem. 10:239-249(2005). CC -!- FUNCTION: Involved in hydrogen uptake for the anaerobic reduction of CC sulfate to hydrogen sulfide in an electron transport chain. Cytochrome CC c3 is the physiological electron acceptor. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 Fe(III)-[cytochrome c3] + H2 = 2 Fe(II)-[cytochrome c3] + 2 CC H(+); Xref=Rhea:RHEA:20625, Rhea:RHEA-COMP:11576, Rhea:RHEA- CC COMP:11577, ChEBI:CHEBI:15378, ChEBI:CHEBI:18276, ChEBI:CHEBI:29033, CC ChEBI:CHEBI:29034; EC=1.12.2.1; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Note=Binds 2 [4Fe-4S] clusters per subunit.; CC -!- COFACTOR: CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; CC Note=Binds 1 [3Fe-4S] cluster per subunit.; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Redox potential: CC E(0) is about +65 mV for the 3Fe-4S, and -340 mV for the 4Fe-4S CC clusters. {ECO:0000269|PubMed:9751716}; CC -!- SUBUNIT: Heterodimer of a large and a small subunit. CC {ECO:0000269|PubMed:15803334, ECO:0000269|PubMed:9751716}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M35333; AAA23371.2; -; Genomic_DNA. DR PIR; JQ0761; S08198. DR PDB; 1FRF; X-ray; 2.70 A; S=51-161, S=163-314. DR PDB; 1YQW; X-ray; 1.83 A; A/B/C=51-314. DR PDB; 1YRQ; X-ray; 2.10 A; A/B/C/D/F/G=51-314. DR PDB; 3CUR; X-ray; 2.40 A; A/B/C=51-314. DR PDB; 3CUS; X-ray; 2.20 A; A/B/C=51-314. DR PDB; 3H3X; X-ray; 2.70 A; A/B/C=51-314. DR PDB; 4UCQ; X-ray; 2.60 A; A/B/C=51-314. DR PDB; 4UCW; X-ray; 2.30 A; A/B/C=51-314. DR PDB; 4UCX; X-ray; 1.95 A; A/B/C=51-314. DR PDB; 4UE2; X-ray; 2.02 A; A/B/C=51-314. DR PDB; 4UE6; X-ray; 2.30 A; A/B/C=51-314. DR PDB; 4UEW; X-ray; 2.08 A; A/B/C=51-314. DR PDB; 4UPE; X-ray; 1.80 A; A/B/C=50-314. DR PDB; 4UPV; X-ray; 1.52 A; A/B=50-314. DR PDB; 4UQL; X-ray; 1.22 A; A/B=50-314. DR PDB; 4UQP; X-ray; 1.42 A; A/B=50-314. DR PDB; 4URH; X-ray; 1.44 A; A/B/C=50-314. DR AlphaFoldDB; P18187; -. DR SMR; P18187; -. DR DIP; DIP-6172N; -. DR MINT; P18187; -. DR BRENDA; 1.12.2.1; 1906. DR EvolutionaryTrace; P18187; -. DR GO; GO:0044569; C:[Ni-Fe] hydrogenase complex; IEA:TreeGrafter. DR GO; GO:0009375; C:ferredoxin hydrogenase complex; IEA:InterPro. DR GO; GO:0016020; C:membrane; IEA:TreeGrafter. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0047806; F:cytochrome-c3 hydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0009055; F:electron transfer activity; IEA:TreeGrafter. DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR GO; GO:0009061; P:anaerobic respiration; IEA:TreeGrafter. DR Gene3D; 4.10.480.10; Cytochrome-c3 hydrogenase, C-terminal domain; 1. DR Gene3D; 3.40.50.700; NADH:ubiquinone oxidoreductase-like, 20kDa subunit; 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 NCBIfam; TIGR00391; hydA; 1. DR NCBIfam; TIGR01409; TAT_signal_seq; 1. DR PANTHER; PTHR30013:SF7; HYDROGENASE-2 SMALL CHAIN; 1. DR PANTHER; PTHR30013; NIFE / NIFESE HYDROGENASE SMALL SUBUNIT FAMILY MEMBER; 1. 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 SUPFAM; SSF56770; HydA/Nqo6-like; 1. DR PROSITE; PS51318; TAT; 1. DR PDBsum; 1FRF; -. DR PDBsum; 1YQW; -. DR PDBsum; 1YRQ; -. DR PDBsum; 3CUR; -. DR PDBsum; 3CUS; -. DR PDBsum; 3H3X; -. DR PDBsum; 4UCQ; -. DR PDBsum; 4UCW; -. DR PDBsum; 4UCX; -. DR PDBsum; 4UE2; -. DR PDBsum; 4UE6; -. DR PDBsum; 4UEW; -. DR PDBsum; 4UPE; -. DR PDBsum; 4UPV; -. DR PDBsum; 4UQL; -. DR PDBsum; 4UQP; -. DR PDBsum; 4URH; -. PE 1: Evidence at protein level; KW 3D-structure; 3Fe-4S; 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; KW Metal-binding; Oxidoreductase; Periplasm; Signal. FT SIGNAL 1..49 FT /note="Tat-type signal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648, FT ECO:0000269|PubMed:2154378" FT CHAIN 50..314 FT /note="Periplasmic [NiFe] hydrogenase small subunit" FT /id="PRO_0000013415" FT BINDING 67 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT BINDING 70 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT BINDING 164 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT BINDING 197 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT BINDING 234 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT BINDING 237 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT BINDING 262 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT BINDING 268 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT BINDING 277 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT BINDING 295 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT BINDING 298 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT MUTAGEN 238 FT /note="P->C: Decreased hydrogen uptake and increased FT hydrogen production." FT /evidence="ECO:0000269|PubMed:9751716" FT HELIX 54..57 FT /evidence="ECO:0007829|PDB:4UQL" FT STRAND 58..63 FT /evidence="ECO:0007829|PDB:4UQL" FT HELIX 69..74 FT /evidence="ECO:0007829|PDB:4UQL" FT TURN 78..81 FT /evidence="ECO:0007829|PDB:1FRF" FT HELIX 85..89 FT /evidence="ECO:0007829|PDB:4UQL" FT STRAND 91..94 FT /evidence="ECO:0007829|PDB:4UQL" FT TURN 96..98 FT /evidence="ECO:0007829|PDB:4UQL" FT HELIX 103..114 FT /evidence="ECO:0007829|PDB:4UQL" FT STRAND 121..129 FT /evidence="ECO:0007829|PDB:4UQL" FT HELIX 131..134 FT /evidence="ECO:0007829|PDB:4UQL" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:4UQL" FT HELIX 144..154 FT /evidence="ECO:0007829|PDB:4UQL" FT STRAND 158..161 FT /evidence="ECO:0007829|PDB:4UQL" FT HELIX 162..167 FT /evidence="ECO:0007829|PDB:4UQL" FT HELIX 170..172 FT /evidence="ECO:0007829|PDB:4UQL" FT HELIX 183..187 FT /evidence="ECO:0007829|PDB:4UQL" FT STRAND 192..194 FT /evidence="ECO:0007829|PDB:4UQL" FT STRAND 196..198 FT /evidence="ECO:0007829|PDB:4UQL" FT HELIX 201..213 FT /evidence="ECO:0007829|PDB:4UQL" FT HELIX 216..218 FT /evidence="ECO:0007829|PDB:4UQL" FT HELIX 226..229 FT /evidence="ECO:0007829|PDB:4UQL" FT STRAND 230..232 FT /evidence="ECO:0007829|PDB:4UQL" FT HELIX 234..236 FT /evidence="ECO:0007829|PDB:4UQL" FT HELIX 240..244 FT /evidence="ECO:0007829|PDB:4UQL" FT STRAND 250..254 FT /evidence="ECO:0007829|PDB:4UE2" FT HELIX 255..258 FT /evidence="ECO:0007829|PDB:4UQL" FT HELIX 264..266 FT /evidence="ECO:0007829|PDB:4UQL" FT HELIX 270..272 FT /evidence="ECO:0007829|PDB:4UQL" FT HELIX 277..280 FT /evidence="ECO:0007829|PDB:4UQL" FT TURN 283..285 FT /evidence="ECO:0007829|PDB:4UQL" FT TURN 288..292 FT /evidence="ECO:0007829|PDB:4UQL" FT HELIX 303..306 FT /evidence="ECO:0007829|PDB:4UQL" SQ SEQUENCE 314 AA; 33621 MW; 48BE00FE51D23A68 CRC64; MNFSVGLGRD DAEKRLVQNG VSRRDFMKFC ATVAAAMGMG PAFAPKVAEA LTAKHRPSVV WLHNAECTGC TEAAIRTIKP YIDALILDTI SLDYQETIMA AAGEAAEAAL HQALEGKDGY YLVVEGGLPT IDGGQWGMVA GHPMIETTKK AAAKAKGIIC IGTCSAYGGV QKAKPNPSQA KGVSEALGVK TINIPGCPPN PINFVGAVVH VLTKGIPDLD ENGRPKLFYG ELVHDNCPRL PHFEASEFAP SFDSEEAKKG FCLYELGCKG PVTYNNCPKV LFNQVNWPVQ AGHPCLGCSE PDFWDTMTPF YEQG //