PHFL_CUPO1
ID PHFL_CUPO1 Reviewed; 421 AA.
AC P13629;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Periplasmic [Fe] hydrogenase large subunit;
DE EC=1.12.7.2;
DE AltName: Full=Fe hydrogenlyase;
GN Name=hydA;
OS Cupidesulfovibrio oxamicus (strain Monticello) (Desulfovibrio vulgaris
OS subsp. oxamicus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Cupidesulfovibrio.
OX NCBI_TaxID=884;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2661538; DOI=10.1128/jb.171.7.3881-3889.1989;
RA Voordouw G., Strang J.D., Wilson F.R.;
RT "Organization of the genes encoding [Fe] hydrogenase in Desulfovibrio
RT vulgaris subsp. oxamicus Monticello.";
RL J. Bacteriol. 171:3881-3889(1989).
CC -!- FUNCTION: May be involved in hydrogen uptake for the reduction of
CC sulfate to hydrogen sulfide in an electron transport chain. Cytochrome
CC c3 is likely to be the physiological electron carrier for the enzyme.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2 + 2 oxidized [2Fe-2S]-[ferredoxin] = 2 H(+) + 2 reduced
CC [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:17445, Rhea:RHEA-COMP:10000,
CC Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:18276,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.12.7.2;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P07598};
CC Note=Binds 3 [4Fe-4S] clusters per subunit.
CC {ECO:0000250|UniProtKB:P07598};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P07598};
CC Note=Contains an active site Fe binuclear center, which is coordinated
CC by Cys-382 and by non-protein ligands. {ECO:0000250|UniProtKB:P07598};
CC -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- MISCELLANEOUS: [Fe], [NiFe], and [NiFeSe] hydrogenases appear to
CC represent three distinct enzymes having hydrogenase activity.
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DR EMBL; M27212; AAA23373.1; -; Genomic_DNA.
DR PIR; A32886; HQDVLV.
DR AlphaFoldDB; P13629; -.
DR SMR; P13629; -.
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:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR009016; Fe_hydrogenase.
DR InterPro; IPR004108; Fe_hydrogenase_lsu_C.
DR InterPro; IPR013352; Fe_hydrogenase_subset.
DR Pfam; PF02906; Fe_hyd_lg_C; 1.
DR Pfam; PF13187; Fer4_9; 1.
DR SUPFAM; SSF53920; SSF53920; 1.
DR TIGRFAMs; TIGR02512; FeFe_hydrog_A; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Oxidoreductase; Periplasm; Repeat; Transport.
FT CHAIN 1..421
FT /note="Periplasmic [Fe] hydrogenase large subunit"
FT /id="PRO_0000159240"
FT DOMAIN 26..55
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 56..86
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 35
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07598"
FT BINDING 38
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07598"
FT BINDING 41
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07598"
FT BINDING 45
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07598"
FT BINDING 66
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07598"
FT BINDING 69
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07598"
FT BINDING 72
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07598"
FT BINDING 76
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07598"
FT BINDING 179
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P07598"
FT BINDING 234
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P07598"
FT BINDING 378
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P07598"
FT BINDING 382
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P07598"
FT BINDING 382
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000250|UniProtKB:P07598"
SQ SEQUENCE 421 AA; 46279 MW; 8E987ABC4DC7C965 CRC64;
MSRIEMEKIF YEDHAPDPKA DPDKLFFIQI DESKCIGCDS CQQYCPTGAI FGDTGDAHKI
PHEELCINCG QCLTHCPVGA IYESQSWVTE IEKKIKAKDV KVIAMPAPAV RYALGDAFGL
PVGTVTTGKM FSALKELGFD HCWDNEFTAD VTIWEEGTEF VQRLTKKLDK PLPQFTSCCP
GWHKYVESLY PELFPHMSSC KSPIGMLGTL AKTYGADRMK YDRAKVYTVS IMPCTAKKYE
GMRPQLWDSG HKDIDATIDT RELAYMIKKA KIDFTKLPDG KRDTLMGEST GGATLFGVTG
GVMEAALRYA YQAVTGKKPE SMDFKGVRGL QGVKEATVNV GGVDVKVAVV HGARRFHDVC
ELVKAGKAPW HFIEFMACPG GCVCGGGQPV MPGVLEAADR RSTRMYAGLK KRLAMASASR
A
