MBHS_CUPNH
ID MBHS_CUPNH Reviewed; 360 AA.
AC P31892;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Uptake hydrogenase small subunit;
DE EC=1.12.99.6;
DE AltName: Full=Hydrogenlyase;
DE AltName: Full=Membrane-bound hydrogenase small subunit;
DE Flags: Precursor;
GN Name=hoxK; OrderedLocusNames=PHG001;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OG Plasmid megaplasmid pHG1.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1383192; DOI=10.1128/jb.174.19.6277-6289.1992;
RA Kortlueke C., Horstmann K., Schwartz E., Rohde M., Binsack R.,
RA Friedrich B.;
RT "A gene complex coding for the membrane-bound hydrogenase of Alcaligenes
RT eutrophus H16.";
RL J. Bacteriol. 174:6277-6289(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=12948488; DOI=10.1016/s0022-2836(03)00894-5;
RA Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.;
RT "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid
RT encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis.";
RL J. Mol. Biol. 332:369-383(2003).
RN [3]
RP PROTEIN SEQUENCE OF 44-59.
RX PubMed=2493816; DOI=10.1016/0167-4838(89)90225-2;
RA Lorenz B., Schneider K., Kratzin H., Schlegel H.G.;
RT "Immunological comparison of subunits isolated from various hydrogenases of
RT aerobic hydrogen bacteria.";
RL Biochim. Biophys. Acta 995:1-9(1989).
CC -!- FUNCTION: This enzyme recycles the H(2) produced by nitrogenase to
CC increase the production of ATP and to protect nitrogenase against
CC inhibition or damage by O(2) under carbon- or phosphate-limited
CC conditions.
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=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250};
CC -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC -!- INTERACTION:
CC P31892; P31891: hoxG; NbExp=3; IntAct=EBI-15948434, EBI-15948409;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
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; M96433; AAA16461.1; -; Unassigned_DNA.
DR EMBL; AY305378; AAP85757.1; -; Genomic_DNA.
DR PIR; A43255; A43255.
DR RefSeq; WP_011153926.1; NZ_CP039289.1.
DR PDB; 3RGW; X-ray; 1.50 A; S=44-360.
DR PDB; 4IUB; X-ray; 1.61 A; S=44-360.
DR PDB; 4IUC; X-ray; 1.45 A; S=44-360.
DR PDB; 4IUD; X-ray; 1.45 A; S=44-360.
DR PDB; 4TTT; X-ray; 1.72 A; S=44-360.
DR PDB; 5D51; X-ray; 1.47 A; S=44-360.
DR PDB; 5MDJ; X-ray; 1.48 A; S=44-360.
DR PDB; 5MDK; X-ray; 1.50 A; S=44-360.
DR PDB; 5MDL; X-ray; 1.41 A; S=44-360.
DR PDB; 7ODG; X-ray; 1.62 A; S=44-360.
DR PDB; 7ODH; X-ray; 1.34 A; S=44-360.
DR PDBsum; 3RGW; -.
DR PDBsum; 4IUB; -.
DR PDBsum; 4IUC; -.
DR PDBsum; 4IUD; -.
DR PDBsum; 4TTT; -.
DR PDBsum; 5D51; -.
DR PDBsum; 5MDJ; -.
DR PDBsum; 5MDK; -.
DR PDBsum; 5MDL; -.
DR PDBsum; 7ODG; -.
DR PDBsum; 7ODH; -.
DR AlphaFoldDB; P31892; -.
DR SMR; P31892; -.
DR DIP; DIP-59145N; -.
DR IntAct; P31892; 1.
DR STRING; 381666.PHG001; -.
DR EnsemblBacteria; AAP85757; AAP85757; PHG001.
DR GeneID; 39976570; -.
DR KEGG; reh:PHG001; -.
DR PATRIC; fig|381666.6.peg.1; -.
DR eggNOG; COG1740; Bacteria.
DR HOGENOM; CLU_046107_0_0_4; -.
DR OMA; PLNQDGM; -.
DR OrthoDB; 798037at2; -.
DR BioCyc; MetaCyc:HOXKALCA-MON; -.
DR Proteomes; UP000008210; Plasmid megaplasmid pHG1.
DR GO; GO:0009375; C:ferredoxin hydrogenase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; 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; 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; 3Fe-4S; 4Fe-4S; Cell membrane; Direct protein sequencing;
KW Iron; Iron-sulfur; Membrane; Metal-binding; Oxidoreductase; Plasmid;
KW Reference proteome; Signal.
FT SIGNAL 1..43
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:2493816"
FT CHAIN 44..360
FT /note="Uptake hydrogenase small subunit"
FT /id="PRO_0000013421"
FT BINDING 60
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:7ODH"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 75..81
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:7ODH"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:7ODH"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 156..160
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 196..209
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 236..240
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:7ODH"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:5MDL"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:7ODH"
FT TURN 279..282
FT /evidence="ECO:0007829|PDB:7ODH"
FT TURN 285..289
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:7ODH"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:5MDL"
SQ SEQUENCE 360 AA; 39472 MW; D2BB15D85902AF0C CRC64;
MVETFYEVMR RQGISRRSFL KYCSLTATSL GLGPSFLPQI AHAMETKPRT PVLWLHGLEC
TCCSESFIRS AHPLAKDVVL SMISLDYDDT LMAAAGHQAE AILEEIMTKY KGNYILAVEG
NPPLNQDGMS CIIGGRPFIE QLKYVAKDAK AIISWGSCAS WGCVQAAKPN PTQATPVHKV
ITDKPIIKVP GCPPIAEVMT GVITYMLTFD RIPELDRQGR PKMFYSQRIH DKCYRRPHFD
AGQFVEEWDD ESARKGFCLY KMGCKGPTTY NACSTTRWNE GTSFPIQSGH GCIGCSEDGF
WDKGSFYDRL TGISQFGVEA NADKIGGTAS VVVGAAVTAH AAASAIKRAS KKNETSGSEH
