PHF1_CLOPA
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 03-AUG-2022, entry version 144.
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; Eubacteriales; 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] {ECO:0007744|PDB:1FEH}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH A BINUCLEAR IRON
RP CENTER; IRON-SULFUR (2FE-2S) AND IRON-SULFUR (4FE-4S) CLUSTERS, AND
RP COFACTOR.
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 Clostridium
RT pasteurianum to 1.8-A resolution.";
RL Science 282:1853-1858(1998).
RN [3] {ECO:0007744|PDB:1C4A, ECO:0007744|PDB:1C4C}
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH A BINUCLEAR IRON
RP CENTER; IRON-SULFUR (2FE-2S) AND IRON-SULFUR (4FE-4S) CLUSTERS, AND
RP COFACTOR.
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 the
RT 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 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=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:10529166, ECO:0000269|PubMed:9836629};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000269|PubMed:10529166, ECO:0000269|PubMed:9836629};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:10529166, ECO:0000269|PubMed:9836629};
CC Note=Binds 4 [4Fe-4S] clusters per subunit.
CC {ECO:0000269|PubMed:10529166, ECO:0000269|PubMed:9836629};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:10529166, ECO:0000269|PubMed:9836629};
CC Note=Contains an active site Fe binuclear center, which is coordinated
CC by Cys-503 and by non-protein ligands including 2 sulfur atoms, 1 water
CC and 5 cyanide or carbon monoxide ligands.
CC {ECO:0000269|PubMed:10529166};
CC -!- SUBUNIT: Monomer.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 PDB; 6H63; X-ray; 2.08 A; A/B=1-574.
DR PDB; 6N59; X-ray; 1.02 A; A=1-574.
DR PDB; 6N6P; X-ray; 1.95 A; A=1-574.
DR PDB; 6NAC; X-ray; 1.55 A; A=1-574.
DR PDB; 6YF4; X-ray; 1.77 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 PDBsum; 6H63; -.
DR PDBsum; 6N59; -.
DR PDBsum; 6N6P; -.
DR PDBsum; 6NAC; -.
DR PDBsum; 6YF4; -.
DR AlphaFoldDB; P29166; -.
DR SMR; P29166; -.
DR KEGG; ag:AAA23248; -.
DR EvolutionaryTrace; P29166; -.
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 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
FT /note="Iron hydrogenase 1"
FT /id="PRO_0000199732"
FT DOMAIN 1..78
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 78..117
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT DOMAIN 138..167
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 181..210
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 34
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:10529166,
FT ECO:0000269|PubMed:9836629"
FT BINDING 46
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:10529166,
FT ECO:0000269|PubMed:9836629"
FT BINDING 49
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:10529166,
FT ECO:0000269|PubMed:9836629"
FT BINDING 62
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:10529166,
FT ECO:0000269|PubMed:9836629"
FT BINDING 94
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184,
FT ECO:0000269|PubMed:10529166"
FT BINDING 98
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184,
FT ECO:0000269|PubMed:10529166, ECO:0000269|PubMed:9836629"
FT BINDING 101
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184,
FT ECO:0000269|PubMed:10529166, ECO:0000269|PubMed:9836629"
FT BINDING 107
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184,
FT ECO:0000269|PubMed:10529166, ECO:0000269|PubMed:9836629"
FT BINDING 147
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10529166,
FT ECO:0000269|PubMed:9836629"
FT BINDING 150
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10529166,
FT ECO:0000269|PubMed:9836629"
FT BINDING 153
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10529166,
FT ECO:0000269|PubMed:9836629"
FT BINDING 157
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10529166,
FT ECO:0000269|PubMed:9836629"
FT BINDING 190
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10529166,
FT ECO:0000269|PubMed:9836629"
FT BINDING 193
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10529166,
FT ECO:0000269|PubMed:9836629"
FT BINDING 196
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10529166,
FT ECO:0000269|PubMed:9836629"
FT BINDING 200
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10529166,
FT ECO:0000269|PubMed:9836629"
FT BINDING 300
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:10529166,
FT ECO:0000269|PubMed:9836629"
FT BINDING 355
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:10529166,
FT ECO:0000269|PubMed:9836629"
FT BINDING 499
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:10529166,
FT ECO:0000269|PubMed:9836629"
FT BINDING 503
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:10529166,
FT ECO:0000269|PubMed:9836629"
FT BINDING 503
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000269|PubMed:10529166"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:6N59"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:6N59"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:6N59"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:6N59"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:6N59"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:6N59"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 77..91
FT /evidence="ECO:0007829|PDB:6N59"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:1C4A"
FT TURN 102..105
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:6N59"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 152..161
FT /evidence="ECO:0007829|PDB:6N59"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:6N59"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:6N59"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:6N59"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 237..241
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 250..259
FT /evidence="ECO:0007829|PDB:6N59"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 268..289
FT /evidence="ECO:0007829|PDB:6N59"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:4XDD"
FT HELIX 301..310
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 312..317
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 324..332
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 335..340
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:6N59"
FT STRAND 347..354
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 357..362
FT /evidence="ECO:0007829|PDB:6N59"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:6N59"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:6N59"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 381..390
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:6N59"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 422..436
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:6N59"
FT STRAND 453..461
FT /evidence="ECO:0007829|PDB:6N59"
FT STRAND 464..473
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 474..482
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 485..487
FT /evidence="ECO:0007829|PDB:6N59"
FT STRAND 493..499
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 503..505
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 514..519
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 522..536
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 542..544
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 546..554
FT /evidence="ECO:0007829|PDB:6N59"
FT HELIX 562..567
FT /evidence="ECO:0007829|PDB:6N59"
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
