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Database: UniProt
Entry: P13629
LinkDB: P13629
Original site: P13629 
ID   PHFL_DESOM              Reviewed;         421 AA.
AC   P13629;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   05-DEC-2018, entry version 90.
DE   RecName: Full=Periplasmic [Fe] hydrogenase large subunit;
DE            EC=1.12.7.2;
DE   AltName: Full=Fe hydrogenlyase;
GN   Name=hydA;
OS   Desulfovibrio oxamicus (strain Monticello) (Desulfovibrio vulgaris
OS   subsp. oxamicus).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
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.
CC       Cytochrome c3 is likely to be the physiological electron carrier
CC       for the enzyme.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2 + 2 oxidized [2Fe-2S]-[ferredoxin] = 2 H(+) + 2
CC         reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:17445, Rhea:RHEA-
CC         COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:18276, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738;
CC         EC=1.12.7.2;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250};
CC       Note=Binds 3 [4Fe-4S] clusters per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 2 iron ions per subunit. {ECO:0000250};
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.
DR   EMBL; M27212; AAA23373.1; -; Genomic_DNA.
DR   PIR; A32886; HQDVLV.
DR   ProteinModelPortal; 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       Periplasmic [Fe] hydrogenase large
FT                                subunit.
FT                                /FTId=PRO_0000159240.
FT   DOMAIN       26     55       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       56     86       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        35     35       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        38     38       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        41     41       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        45     45       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        66     66       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        69     69       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        72     72       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        76     76       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL       179    179       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       234    234       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       378    378       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       382    382       Diiron subcluster. {ECO:0000250}.
FT   METAL       382    382       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
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
//
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