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Protein

Iron hydrogenase 1

Gene
N/A
Organism
Clostridium pasteurianum
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

H2 + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H+.

Cofactori

Protein has several cofactor binding sites:
  • [2Fe-2S] clusterNote: Binds 1 [2Fe-2S] cluster per subunit.
  • [4Fe-4S] clusterNote: Binds 4 [4Fe-4S] clusters per subunit.
  • Fe cationNote: Binds 2 iron ions per subunit. Besides cysteine ligand the diiron subcluster contains non-protein ligands including 2 sulfur atoms, 1 water and 5 cyanide or carbon monoxide ligands.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi34 – 341Iron-sulfur 1 (2Fe-2S)1 Publication
Metal bindingi46 – 461Iron-sulfur 1 (2Fe-2S)1 Publication
Metal bindingi49 – 491Iron-sulfur 1 (2Fe-2S)1 Publication
Metal bindingi62 – 621Iron-sulfur 1 (2Fe-2S)1 Publication
Metal bindingi94 – 941Iron-sulfur 2 (4Fe-4S); via tele nitrogen
Metal bindingi98 – 981Iron-sulfur 2 (4Fe-4S)1 Publication
Metal bindingi101 – 1011Iron-sulfur 2 (4Fe-4S)1 Publication
Metal bindingi107 – 1071Iron-sulfur 2 (4Fe-4S)1 Publication
Metal bindingi147 – 1471Iron-sulfur 3 (4Fe-4S)1 Publication
Metal bindingi150 – 1501Iron-sulfur 3 (4Fe-4S)1 Publication
Metal bindingi153 – 1531Iron-sulfur 3 (4Fe-4S)1 Publication
Metal bindingi157 – 1571Iron-sulfur 4 (4Fe-4S)1 Publication
Metal bindingi190 – 1901Iron-sulfur 4 (4Fe-4S)1 Publication
Metal bindingi193 – 1931Iron-sulfur 4 (4Fe-4S)1 Publication
Metal bindingi196 – 1961Iron-sulfur 4 (4Fe-4S)1 Publication
Metal bindingi200 – 2001Iron-sulfur 3 (4Fe-4S)1 Publication
Metal bindingi300 – 3001Iron-sulfur 5 (4Fe-4S)1 Publication
Metal bindingi355 – 3551Iron-sulfur 5 (4Fe-4S)1 Publication
Metal bindingi499 – 4991Iron-sulfur 5 (4Fe-4S)1 Publication
Metal bindingi503 – 5031Diiron subcluster
Metal bindingi503 – 5031Iron-sulfur 5 (4Fe-4S)1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Iron hydrogenase 1 (EC:1.12.7.2)
Alternative name(s):
CpI
Fe-only hydrogenase
[Fe] hydrogenase
OrganismiClostridium pasteurianum
Taxonomic identifieri1501 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Pathology & Biotechi

Chemistry

DrugBankiDB00916. Metronidazole.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 574574Iron hydrogenase 1PRO_0000199732Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
574
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Beta strandi9 – 135Combined sources
Helixi19 – 257Combined sources
Beta strandi42 – 443Combined sources
Beta strandi50 – 534Combined sources
Turni54 – 563Combined sources
Beta strandi57 – 604Combined sources
Helixi61 – 633Combined sources
Beta strandi71 – 755Combined sources
Helixi77 – 9115Combined sources
Turni98 – 1003Combined sources
Turni102 – 1054Combined sources
Helixi108 – 1169Combined sources
Helixi129 – 1324Combined sources
Beta strandi137 – 1437Combined sources
Helixi144 – 1463Combined sources
Helixi152 – 16110Combined sources
Beta strandi166 – 1716Combined sources
Beta strandi174 – 1796Combined sources
Helixi180 – 1823Combined sources
Helixi185 – 1873Combined sources
Helixi195 – 1995Combined sources
Beta strandi205 – 2073Combined sources
Helixi211 – 2199Combined sources
Beta strandi224 – 2296Combined sources
Helixi231 – 2355Combined sources
Helixi237 – 2415Combined sources
Helixi250 – 26011Combined sources
Beta strandi263 – 2675Combined sources
Helixi268 – 28922Combined sources
Beta strandi292 – 2965Combined sources
Helixi301 – 31010Combined sources
Helixi312 – 3176Combined sources
Helixi324 – 3329Combined sources
Helixi335 – 3384Combined sources
Turni339 – 3413Combined sources
Helixi344 – 3463Combined sources
Beta strandi347 – 3548Combined sources
Helixi357 – 3626Combined sources
Beta strandi367 – 3693Combined sources
Beta strandi372 – 3743Combined sources
Beta strandi376 – 3805Combined sources
Helixi381 – 39010Combined sources
Helixi395 – 3973Combined sources
Helixi405 – 4073Combined sources
Helixi412 – 4154Combined sources
Turni416 – 4183Combined sources
Helixi422 – 43615Combined sources
Helixi446 – 4483Combined sources
Beta strandi453 – 4619Combined sources
Beta strandi464 – 47310Combined sources
Helixi474 – 4829Combined sources
Helixi485 – 4873Combined sources
Beta strandi493 – 4997Combined sources
Helixi503 – 5053Combined sources
Helixi514 – 5196Combined sources
Helixi522 – 53615Combined sources
Helixi542 – 5443Combined sources
Helixi546 – 5549Combined sources
Helixi562 – 5676Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C4AX-ray2.40A1-574[»]
1C4CX-ray2.40A1-574[»]
1FEHX-ray1.80A1-574[»]
3C8YX-ray1.39A1-574[»]
4XDCX-ray1.63A/B1-574[»]
4XDDX-ray1.60A/B1-574[»]
5BYQX-ray1.73A/B1-574[»]
5BYRX-ray1.82A/B1-574[»]
5BYSX-ray1.93A/B1-574[»]
ProteinModelPortaliP29166.
SMRiP29166. Positions 1-574.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29166.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 78782Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini138 – 167304Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini181 – 210304Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 2 4Fe-4S ferredoxin-type domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di4.10.260.20. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR009016. Fe_hydrogenase.
IPR004108. Fe_hydrogenase_lsu_C.
IPR003149. Fe_hydrogenase_ssu.
IPR013352. Fe_hydrogenase_subset.
[Graphical view]
PfamiPF02906. Fe_hyd_lg_C. 1 hit.
PF02256. Fe_hyd_SSU. 1 hit.
PF12838. Fer4_7. 1 hit.
[Graphical view]
SMARTiSM00902. Fe_hyd_SSU. 1 hit.
[Graphical view]
SUPFAMiSSF53920. SSF53920. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR02512. FeFe_hydrog_A. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
PS00198. 4FE4S_FER_1. 2 hits.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29166-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTIIINGVQ FNTDEDTTIL KFARDNNIDI SALCFLNNCN NDINKCEICT
60 70 80 90 100
VEVEGTGLVT ACDTLIEDGM IINTNSDAVN EKIKSRISQL LDIHEFKCGP
110 120 130 140 150
CNRRENCEFL KLVIKYKARA SKPFLPKDKT EYVDERSKSL TVDRTKCLLC
160 170 180 190 200
GRCVNACGKN TETYAMKFLN KNGKTIIGAE DEKCFDDTNC LLCGQCIIAC
210 220 230 240 250
PVAALSEKSH MDRVKNALNA PEKHVIVAMA PSVRASIGEL FNMGFGVDVT
260 270 280 290 300
GKIYTALRQL GFDKIFDINF GADMTIMEEA TELVQRIENN GPFPMFTSCC
310 320 330 340 350
PGWVRQAENY YPELLNNLSS AKSPQQIFGT ASKTYYPSIS GLDPKNVFTV
360 370 380 390 400
TVMPCTSKKF EADRPQMEKD GLRDIDAVIT TRELAKMIKD AKIPFAKLED
410 420 430 440 450
SEADPAMGEY SGAGAIFGAT GGVMEAALRS AKDFAENAEL EDIEYKQVRG
460 470 480 490 500
LNGIKEAEVE INNNKYNVAV INGASNLFKF MKSGMINEKQ YHFIEVMACH
510 520 530 540 550
GGCVNGGGQP HVNPKDLEKV DIKKVRASVL YNQDEHLSKR KSHENTALVK
560 570
MYQNYFGKPG EGRAHEILHF KYKK
Length:574
Mass (Da):63,828
Last modified:December 1, 1992 - v1
Checksum:i17E28A74E23C7DEE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81737 Genomic DNA. Translation: AAA23248.1.
PIRiA40330. HQCL1P.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81737 Genomic DNA. Translation: AAA23248.1.
PIRiA40330. HQCL1P.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C4AX-ray2.40A1-574[»]
1C4CX-ray2.40A1-574[»]
1FEHX-ray1.80A1-574[»]
3C8YX-ray1.39A1-574[»]
4XDCX-ray1.63A/B1-574[»]
4XDDX-ray1.60A/B1-574[»]
5BYQX-ray1.73A/B1-574[»]
5BYRX-ray1.82A/B1-574[»]
5BYSX-ray1.93A/B1-574[»]
ProteinModelPortaliP29166.
SMRiP29166. Positions 1-574.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

DrugBankiDB00916. Metronidazole.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP29166.

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di4.10.260.20. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR009016. Fe_hydrogenase.
IPR004108. Fe_hydrogenase_lsu_C.
IPR003149. Fe_hydrogenase_ssu.
IPR013352. Fe_hydrogenase_subset.
[Graphical view]
PfamiPF02906. Fe_hyd_lg_C. 1 hit.
PF02256. Fe_hyd_SSU. 1 hit.
PF12838. Fer4_7. 1 hit.
[Graphical view]
SMARTiSM00902. Fe_hyd_SSU. 1 hit.
[Graphical view]
SUPFAMiSSF53920. SSF53920. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR02512. FeFe_hydrog_A. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
PS00198. 4FE4S_FER_1. 2 hits.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPHF1_CLOPA
AccessioniPrimary (citable) accession number: P29166
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: September 7, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.