PHNL_SOLFR
ID PHNL_SOLFR Reviewed; 564 AA.
AC P18188;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 4.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Periplasmic [NiFe] hydrogenase large subunit;
DE EC=1.12.2.1;
DE AltName: Full=NiFe hydrogenlyase large chain;
DE Flags: Precursor;
GN Name=hydB;
OS Solidesulfovibrio fructosivorans (Desulfovibrio fructosivorans).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC 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 2-20.
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).
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=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Note=Binds 1 nickel ion per subunit.;
CC -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- MISCELLANEOUS: Perhaps the leader of the small subunit serves as a
CC transport vehicle for both subunits.
CC -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC family. {ECO:0000305}.
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DR EMBL; M35333; AAA23372.2; -; Genomic_DNA.
DR PIR; JQ0762; S08199.
DR PDB; 1FRF; X-ray; 2.70 A; L=1-564.
DR PDB; 1YQW; X-ray; 1.83 A; Q/R/S=1-549.
DR PDB; 1YRQ; X-ray; 2.10 A; H/I/J/K/M/N=1-549.
DR PDB; 3CUR; X-ray; 2.40 A; H/I/J=1-549.
DR PDB; 3CUS; X-ray; 2.20 A; Q/R/S=1-549.
DR PDB; 3H3X; X-ray; 2.70 A; Q/R/S=1-549.
DR PDB; 4UCQ; X-ray; 2.60 A; Q/R/S=2-549.
DR PDB; 4UCW; X-ray; 2.30 A; Q/R/S=2-549.
DR PDB; 4UCX; X-ray; 1.95 A; Q/R/S=2-549.
DR PDB; 4UE2; X-ray; 2.02 A; Q/R/S=1-549.
DR PDB; 4UE6; X-ray; 2.30 A; Q/R/S=1-549.
DR PDB; 4UEW; X-ray; 2.08 A; Q/R/S=1-549.
DR PDB; 4UPE; X-ray; 1.80 A; Q/R/S=2-549.
DR PDB; 4UPV; X-ray; 1.52 A; Q/R=2-549.
DR PDB; 4UQL; X-ray; 1.22 A; Q/R=2-549.
DR PDB; 4UQP; X-ray; 1.42 A; Q/R=2-549.
DR PDB; 4URH; X-ray; 1.44 A; Q/R/S=2-549.
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; -.
DR AlphaFoldDB; P18188; -.
DR SMR; P18188; -.
DR DIP; DIP-6171N; -.
DR MINT; P18188; -.
DR EvolutionaryTrace; P18188; -.
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:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR Gene3D; 1.10.645.10; -; 1.
DR InterPro; IPR001501; Ni-dep_hyd_lsu.
DR InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS.
DR InterPro; IPR029014; NiFe-Hase_large.
DR Pfam; PF00374; NiFeSe_Hases; 1.
DR SUPFAM; SSF56762; SSF56762; 1.
DR PROSITE; PS00507; NI_HGENASE_L_1; 1.
DR PROSITE; PS00508; NI_HGENASE_L_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Metal-binding; Nickel;
KW Oxidoreductase; Periplasm.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2154378"
FT CHAIN 2..549
FT /note="Periplasmic [NiFe] hydrogenase large subunit"
FT /id="PRO_0000013401"
FT PROPEP 550..564
FT /evidence="ECO:0000250"
FT /id="PRO_0000013402"
FT BINDING 72
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 75
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 543
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 546
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:4UQL"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:4UQL"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:4UQL"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 64..68
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:4UQL"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 97..121
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 157..172
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:4UQL"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 195..223
FT /evidence="ECO:0007829|PDB:4UQL"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:4UQL"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:3CUR"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 245..264
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 266..276
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 278..282
FT /evidence="ECO:0007829|PDB:4UQL"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:4UQL"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 302..308
FT /evidence="ECO:0007829|PDB:4UQL"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:4UQL"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:4UQL"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:4UQL"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:4UQL"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:1FRF"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:4UQL"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:4UQL"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:4UCW"
FT HELIX 385..394
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 398..411
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 415..418
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 421..452
FT /evidence="ECO:0007829|PDB:4UQL"
FT STRAND 464..474
FT /evidence="ECO:0007829|PDB:4UQL"
FT STRAND 477..486
FT /evidence="ECO:0007829|PDB:4UQL"
FT STRAND 489..496
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 498..503
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 514..519
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 531..539
FT /evidence="ECO:0007829|PDB:4UQL"
FT HELIX 544..548
FT /evidence="ECO:0007829|PDB:4UQL"
SQ SEQUENCE 564 AA; 61436 MW; AB3EBF47F364D849 CRC64;
MAESKPTPQS TFTGPIVVDP ITRIEGHLRI MVEVENGKVK DAWSSSQLFR GLEIILKGRD
PRDAQHFTQR ACGVCTYVHA LASSRCVDDA VKVSIPANAR MMRNLVMASQ YLHDHLVHFY
HLHALDWVDV TAALKADPNK AAKLAASIAP ARPGNSAKAL KAVQDKLKAF VESGQLGIFT
NAYFLGGHKA YYLPPEVDLI ATAHYLEALH MQVKAASAMA ILGGKNPHTQ FTVVGGCSNY
QGLTKDPLAN YLALSKEVCQ FVNECYIPDL LAVAGFYKDW GGIGGTSNYL AFGEFATDDS
SPEKHLATSQ FPSGVITGRD LGKVDNVDLG AIYEDVKYSW YAPGGDGKHP YDGVTDPKYT
KLDDKDHYSW MKAPRYKGKA MEVGPLARTF IAYAKGQPDF KKVVDMVLGK LSVPATALHS
TLGRTAARGI ETAIVCANME KWIKEMADSG AKDNTLCAKW EMPEESKGVG LADAPRGALS
HWIRIKGKKI DNFQLVVPST WNLGPRGAQG DKSPVEEALI GTPIADPKRP VEILRTVHAF
DPCIACGVHV IEPETNEILK FKVC
