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Database: UniProt
Entry: P29166
LinkDB: P29166
Original site: P29166 
ID   PHF1_CLOPA              Reviewed;         574 AA.
AC   P29166;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   16-JAN-2019, entry version 132.
DE   RecName: Full=Iron hydrogenase 1;
DE            EC=1.12.7.2;
DE   AltName: Full=CpI;
DE   AltName: Full=Fe-only hydrogenase;
DE   AltName: Full=[Fe] hydrogenase;
OS   Clostridium pasteurianum.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1501;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 6013 / DSM 525 / NCIB 9486 / VKM B-1774 / W5;
RX   PubMed=1911757; DOI=10.1021/bi00104a018;
RA   Meyer J., Gagnon J.;
RT   "Primary structure of hydrogenase I from Clostridium pasteurianum.";
RL   Biochemistry 30:9697-9704(1991).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   PubMed=9836629; DOI=10.1126/science.282.5395.1853;
RA   Peters J.W., Lanzilotta W.N., Lemon B.J., Seefeldt L.C.;
RT   "X-ray crystal structure of the Fe-only hydrogenase (CpI) from
RT   Clostridium pasteurianum to 1.8-A resolution.";
RL   Science 282:1853-1858(1998).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX   PubMed=10529166; DOI=10.1021/bi9913193;
RA   Lemon B.J., Peters J.W.;
RT   "Binding of exogenously added carbon monoxide at the active site of
RT   the iron-only hydrogenase (CpI) from Clostridium pasteurianum.";
RL   Biochemistry 38:12969-12973(1999).
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=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
CC       Note=Binds 1 [2Fe-2S] cluster per subunit.;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 4 [4Fe-4S] clusters per subunit.;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC       Note=Binds 2 iron ions per subunit. Besides cysteine ligand the
CC       diiron subcluster contains non-protein ligands including 2 sulfur
CC       atoms, 1 water and 5 cyanide or carbon monoxide ligands.;
CC   -!- SUBUNIT: Monomer.
DR   EMBL; M81737; AAA23248.1; -; Genomic_DNA.
DR   PIR; A40330; HQCL1P.
DR   RefSeq; WP_004455619.1; NZ_LFYL01000002.1.
DR   PDB; 1C4A; X-ray; 2.40 A; A=1-574.
DR   PDB; 1C4C; X-ray; 2.40 A; A=1-574.
DR   PDB; 1FEH; X-ray; 1.80 A; A=1-574.
DR   PDB; 3C8Y; X-ray; 1.39 A; A=1-574.
DR   PDB; 4XDC; X-ray; 1.63 A; A/B=1-574.
DR   PDB; 4XDD; X-ray; 1.60 A; A/B=1-574.
DR   PDB; 5BYQ; X-ray; 1.73 A; A/B=1-574.
DR   PDB; 5BYR; X-ray; 1.82 A; A/B=1-574.
DR   PDB; 5BYS; X-ray; 1.93 A; A/B=1-574.
DR   PDB; 5LA3; X-ray; 2.29 A; A/B=2-574.
DR   PDB; 5OEF; X-ray; 2.05 A; A/B=1-574.
DR   PDB; 6GLY; X-ray; 2.09 A; A/B=1-574.
DR   PDB; 6GLZ; X-ray; 2.02 A; A/B=1-574.
DR   PDB; 6GM0; X-ray; 2.11 A; A/B=1-574.
DR   PDB; 6GM1; X-ray; 2.05 A; A/B=1-574.
DR   PDB; 6GM2; X-ray; 2.76 A; A/B=1-574.
DR   PDB; 6GM3; X-ray; 2.22 A; A/B=1-574.
DR   PDB; 6GM4; X-ray; 1.97 A; A/B=1-574.
DR   PDB; 6GM8; X-ray; 1.96 A; A/B=1-574.
DR   PDBsum; 1C4A; -.
DR   PDBsum; 1C4C; -.
DR   PDBsum; 1FEH; -.
DR   PDBsum; 3C8Y; -.
DR   PDBsum; 4XDC; -.
DR   PDBsum; 4XDD; -.
DR   PDBsum; 5BYQ; -.
DR   PDBsum; 5BYR; -.
DR   PDBsum; 5BYS; -.
DR   PDBsum; 5LA3; -.
DR   PDBsum; 5OEF; -.
DR   PDBsum; 6GLY; -.
DR   PDBsum; 6GLZ; -.
DR   PDBsum; 6GM0; -.
DR   PDBsum; 6GM1; -.
DR   PDBsum; 6GM2; -.
DR   PDBsum; 6GM3; -.
DR   PDBsum; 6GM4; -.
DR   PDBsum; 6GM8; -.
DR   ProteinModelPortal; P29166; -.
DR   SMR; P29166; -.
DR   DrugBank; DB00916; Metronidazole.
DR   KEGG; ag:AAA23248; -.
DR   KO; K00532; -.
DR   EvolutionaryTrace; P29166; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 4.10.260.20; -; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
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; IPR003149; Fe_hydrogenase_ssu.
DR   InterPro; IPR036991; Fe_hydrogenase_ssu_sf.
DR   InterPro; IPR013352; Fe_hydrogenase_subset.
DR   InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR   Pfam; PF02906; Fe_hyd_lg_C; 1.
DR   Pfam; PF02256; Fe_hyd_SSU; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   SMART; SM00902; Fe_hyd_SSU; 1.
DR   SUPFAM; SSF53920; SSF53920; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   TIGRFAMs; TIGR02512; FeFe_hydrog_A; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS51839; 4FE4S_HC3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur;
KW   Metal-binding; Oxidoreductase; Repeat.
FT   CHAIN         1    574       Iron hydrogenase 1.
FT                                /FTId=PRO_0000199732.
FT   DOMAIN        1     78       2Fe-2S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   DOMAIN       78    117       4Fe-4S His(Cys)3-ligated-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01184}.
FT   DOMAIN      138    167       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      181    210       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        34     34       Iron-sulfur 1 (2Fe-2S).
FT                                {ECO:0000269|PubMed:9836629}.
FT   METAL        46     46       Iron-sulfur 1 (2Fe-2S).
FT                                {ECO:0000269|PubMed:9836629}.
FT   METAL        49     49       Iron-sulfur 1 (2Fe-2S).
FT                                {ECO:0000269|PubMed:9836629}.
FT   METAL        62     62       Iron-sulfur 1 (2Fe-2S).
FT                                {ECO:0000269|PubMed:9836629}.
FT   METAL        94     94       Iron-sulfur 2 (4Fe-4S); via tele
FT                                nitrogen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01184}.
FT   METAL        98     98       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU01184,
FT                                ECO:0000269|PubMed:9836629}.
FT   METAL       101    101       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU01184,
FT                                ECO:0000269|PubMed:9836629}.
FT   METAL       107    107       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU01184,
FT                                ECO:0000269|PubMed:9836629}.
FT   METAL       147    147       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000269|PubMed:9836629}.
FT   METAL       150    150       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000269|PubMed:9836629}.
FT   METAL       153    153       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000269|PubMed:9836629}.
FT   METAL       157    157       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000269|PubMed:9836629}.
FT   METAL       190    190       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000269|PubMed:9836629}.
FT   METAL       193    193       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000269|PubMed:9836629}.
FT   METAL       196    196       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000269|PubMed:9836629}.
FT   METAL       200    200       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000269|PubMed:9836629}.
FT   METAL       300    300       Iron-sulfur 5 (4Fe-4S).
FT                                {ECO:0000269|PubMed:9836629}.
FT   METAL       355    355       Iron-sulfur 5 (4Fe-4S).
FT                                {ECO:0000269|PubMed:9836629}.
FT   METAL       499    499       Iron-sulfur 5 (4Fe-4S).
FT                                {ECO:0000269|PubMed:9836629}.
FT   METAL       503    503       Diiron subcluster.
FT   METAL       503    503       Iron-sulfur 5 (4Fe-4S).
FT                                {ECO:0000269|PubMed:9836629}.
FT   STRAND        2      6       {ECO:0000244|PDB:3C8Y}.
FT   STRAND        9     13       {ECO:0000244|PDB:3C8Y}.
FT   HELIX        19     25       {ECO:0000244|PDB:3C8Y}.
FT   STRAND       42     44       {ECO:0000244|PDB:3C8Y}.
FT   STRAND       50     53       {ECO:0000244|PDB:3C8Y}.
FT   TURN         54     56       {ECO:0000244|PDB:3C8Y}.
FT   STRAND       57     60       {ECO:0000244|PDB:3C8Y}.
FT   HELIX        61     63       {ECO:0000244|PDB:3C8Y}.
FT   STRAND       71     75       {ECO:0000244|PDB:3C8Y}.
FT   HELIX        77     91       {ECO:0000244|PDB:3C8Y}.
FT   TURN         98    100       {ECO:0000244|PDB:1C4A}.
FT   TURN        102    105       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       108    116       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       129    132       {ECO:0000244|PDB:3C8Y}.
FT   STRAND      137    143       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       144    146       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       152    161       {ECO:0000244|PDB:3C8Y}.
FT   STRAND      166    171       {ECO:0000244|PDB:3C8Y}.
FT   STRAND      174    179       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       180    182       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       185    187       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       195    199       {ECO:0000244|PDB:3C8Y}.
FT   STRAND      205    207       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       211    219       {ECO:0000244|PDB:3C8Y}.
FT   STRAND      224    229       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       231    235       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       237    241       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       250    260       {ECO:0000244|PDB:3C8Y}.
FT   STRAND      263    267       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       268    289       {ECO:0000244|PDB:3C8Y}.
FT   STRAND      292    296       {ECO:0000244|PDB:4XDD}.
FT   HELIX       301    310       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       312    317       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       324    332       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       335    338       {ECO:0000244|PDB:3C8Y}.
FT   TURN        339    341       {ECO:0000244|PDB:1C4A}.
FT   HELIX       344    346       {ECO:0000244|PDB:3C8Y}.
FT   STRAND      347    354       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       357    362       {ECO:0000244|PDB:3C8Y}.
FT   STRAND      367    369       {ECO:0000244|PDB:3C8Y}.
FT   STRAND      372    374       {ECO:0000244|PDB:3C8Y}.
FT   STRAND      376    380       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       381    390       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       395    397       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       405    407       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       412    415       {ECO:0000244|PDB:3C8Y}.
FT   TURN        416    418       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       422    436       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       446    448       {ECO:0000244|PDB:3C8Y}.
FT   STRAND      453    461       {ECO:0000244|PDB:3C8Y}.
FT   STRAND      464    473       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       474    482       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       485    487       {ECO:0000244|PDB:3C8Y}.
FT   STRAND      493    499       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       503    505       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       514    519       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       522    536       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       542    544       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       546    554       {ECO:0000244|PDB:3C8Y}.
FT   HELIX       562    567       {ECO:0000244|PDB:3C8Y}.
SQ   SEQUENCE   574 AA;  63828 MW;  17E28A74E23C7DEE CRC64;
     MKTIIINGVQ FNTDEDTTIL KFARDNNIDI SALCFLNNCN NDINKCEICT VEVEGTGLVT
     ACDTLIEDGM IINTNSDAVN EKIKSRISQL LDIHEFKCGP CNRRENCEFL KLVIKYKARA
     SKPFLPKDKT EYVDERSKSL TVDRTKCLLC GRCVNACGKN TETYAMKFLN KNGKTIIGAE
     DEKCFDDTNC LLCGQCIIAC PVAALSEKSH MDRVKNALNA PEKHVIVAMA PSVRASIGEL
     FNMGFGVDVT GKIYTALRQL GFDKIFDINF GADMTIMEEA TELVQRIENN GPFPMFTSCC
     PGWVRQAENY YPELLNNLSS AKSPQQIFGT ASKTYYPSIS GLDPKNVFTV TVMPCTSKKF
     EADRPQMEKD GLRDIDAVIT TRELAKMIKD AKIPFAKLED SEADPAMGEY SGAGAIFGAT
     GGVMEAALRS AKDFAENAEL EDIEYKQVRG LNGIKEAEVE INNNKYNVAV INGASNLFKF
     MKSGMINEKQ YHFIEVMACH GGCVNGGGQP HVNPKDLEKV DIKKVRASVL YNQDEHLSKR
     KSHENTALVK MYQNYFGKPG EGRAHEILHF KYKK
//
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