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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)DescriptionActionsGraphical viewLength
Metal bindingi34Iron-sulfur 1 (2Fe-2S)1 Publication1
Metal bindingi46Iron-sulfur 1 (2Fe-2S)1 Publication1
Metal bindingi49Iron-sulfur 1 (2Fe-2S)1 Publication1
Metal bindingi62Iron-sulfur 1 (2Fe-2S)1 Publication1
Metal bindingi94Iron-sulfur 2 (4Fe-4S); via tele nitrogen1
Metal bindingi98Iron-sulfur 2 (4Fe-4S)1 Publication1
Metal bindingi101Iron-sulfur 2 (4Fe-4S)1 Publication1
Metal bindingi107Iron-sulfur 2 (4Fe-4S)1 Publication1
Metal bindingi147Iron-sulfur 3 (4Fe-4S)1 Publication1
Metal bindingi150Iron-sulfur 3 (4Fe-4S)1 Publication1
Metal bindingi153Iron-sulfur 3 (4Fe-4S)1 Publication1
Metal bindingi157Iron-sulfur 4 (4Fe-4S)1 Publication1
Metal bindingi190Iron-sulfur 4 (4Fe-4S)1 Publication1
Metal bindingi193Iron-sulfur 4 (4Fe-4S)1 Publication1
Metal bindingi196Iron-sulfur 4 (4Fe-4S)1 Publication1
Metal bindingi200Iron-sulfur 3 (4Fe-4S)1 Publication1
Metal bindingi300Iron-sulfur 5 (4Fe-4S)1 Publication1
Metal bindingi355Iron-sulfur 5 (4Fe-4S)1 Publication1
Metal bindingi499Iron-sulfur 5 (4Fe-4S)1 Publication1
Metal bindingi503Diiron subcluster1
Metal bindingi503Iron-sulfur 5 (4Fe-4S)1 Publication1

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 databases

DrugBankiDB00916. Metronidazole.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001997321 – 574Iron hydrogenase 1Add BLAST574

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1574
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Beta strandi9 – 13Combined sources5
Helixi19 – 25Combined sources7
Beta strandi42 – 44Combined sources3
Beta strandi50 – 53Combined sources4
Turni54 – 56Combined sources3
Beta strandi57 – 60Combined sources4
Helixi61 – 63Combined sources3
Beta strandi71 – 75Combined sources5
Helixi77 – 91Combined sources15
Turni98 – 100Combined sources3
Turni102 – 105Combined sources4
Helixi108 – 116Combined sources9
Helixi129 – 132Combined sources4
Beta strandi137 – 143Combined sources7
Helixi144 – 146Combined sources3
Helixi152 – 161Combined sources10
Beta strandi166 – 171Combined sources6
Beta strandi174 – 179Combined sources6
Helixi180 – 182Combined sources3
Helixi185 – 187Combined sources3
Helixi195 – 199Combined sources5
Beta strandi205 – 207Combined sources3
Helixi211 – 219Combined sources9
Beta strandi224 – 229Combined sources6
Helixi231 – 235Combined sources5
Helixi237 – 241Combined sources5
Helixi250 – 260Combined sources11
Beta strandi263 – 267Combined sources5
Helixi268 – 289Combined sources22
Beta strandi292 – 296Combined sources5
Helixi301 – 310Combined sources10
Helixi312 – 317Combined sources6
Helixi324 – 332Combined sources9
Helixi335 – 338Combined sources4
Turni339 – 341Combined sources3
Helixi344 – 346Combined sources3
Beta strandi347 – 354Combined sources8
Helixi357 – 362Combined sources6
Beta strandi367 – 369Combined sources3
Beta strandi372 – 374Combined sources3
Beta strandi376 – 380Combined sources5
Helixi381 – 390Combined sources10
Helixi395 – 397Combined sources3
Helixi405 – 407Combined sources3
Helixi412 – 415Combined sources4
Turni416 – 418Combined sources3
Helixi422 – 436Combined sources15
Helixi446 – 448Combined sources3
Beta strandi453 – 461Combined sources9
Beta strandi464 – 473Combined sources10
Helixi474 – 482Combined sources9
Helixi485 – 487Combined sources3
Beta strandi493 – 499Combined sources7
Helixi503 – 505Combined sources3
Helixi514 – 519Combined sources6
Helixi522 – 536Combined sources15
Helixi542 – 544Combined sources3
Helixi546 – 554Combined sources9
Helixi562 – 567Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29166.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 782Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST78
Domaini138 – 1674Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd BLAST30
Domaini181 – 2104Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd BLAST30

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

Phylogenomic databases

KOiK00532.

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di3.10.20.30. 1 hit.
4.10.260.20. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR012675. Beta-grasp_dom.
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.

Genome annotation databases

KEGGiag:AAA23248.

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

DrugBankiDB00916. Metronidazole.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAA23248.

Phylogenomic databases

KOiK00532.

Miscellaneous databases

EvolutionaryTraceiP29166.

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di3.10.20.30. 1 hit.
4.10.260.20. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR012675. Beta-grasp_dom.
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: November 30, 2016
This is version 120 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.