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Protein

Pyruvate synthase

Gene

por

Organism
Desulfovibrio africanus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the ferredoxin-dependent oxidative decarboxylation of pyruvate. Required for the transfer of electrons from pyruvate to ferredoxin (PubMed:9294422, PubMed:7612653). Ferredoxin I and ferredoxin II, which are single 4Fe-4S cluster ferredoxins are the most effective electron carriers of POR (PubMed:7612653).1 Publication

Catalytic activityi

Pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+.1 Publication

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei31 – 311Pyruvate2 Publications
Sitei31 – 311Important for catalytic activity1 Publication
Binding sitei64 – 641Thiamine pyrophosphate2 Publications
Sitei64 – 641Important for catalytic activity1 Publication
Binding sitei114 – 1141Pyruvate2 Publications
Sitei114 – 1141Important for catalytic activity1 Publication
Metal bindingi689 – 6891Iron-sulfur 1 (4Fe-4S)3 Publications
Metal bindingi692 – 6921Iron-sulfur 1 (4Fe-4S)3 Publications
Metal bindingi695 – 6951Iron-sulfur 1 (4Fe-4S)3 Publications
Metal bindingi699 – 6991Iron-sulfur 2 (4Fe-4S)3 Publications
Metal bindingi745 – 7451Iron-sulfur 2 (4Fe-4S)3 Publications
Metal bindingi748 – 7481Iron-sulfur 2 (4Fe-4S)3 Publications
Metal bindingi751 – 7511Iron-sulfur 2 (4Fe-4S)3 Publications
Metal bindingi755 – 7551Iron-sulfur 1 (4Fe-4S)3 Publications
Metal bindingi812 – 8121Iron-sulfur 3 (4Fe-4S)3 Publications
Metal bindingi815 – 8151Iron-sulfur 3 (4Fe-4S)3 Publications
Binding sitei817 – 8171Thiamine pyrophosphate3 Publications
Metal bindingi840 – 8401Iron-sulfur 3 (4Fe-4S)3 Publications
Binding sitei840 – 8401Thiamine pyrophosphate3 Publications
Metal bindingi963 – 9631Magnesium3 Publications
Metal bindingi983 – 9831Calcium3 Publications
Metal bindingi985 – 9851Calcium3 Publications
Metal bindingi991 – 9911Magnesium3 Publications
Metal bindingi993 – 9931Magnesium; via carbonyl oxygen3 Publications
Sitei996 – 9961Important for catalytic activity1 Publication
Metal bindingi1056 – 10561Calcium; via carbonyl oxygen3 Publications
Metal bindingi1059 – 10591Calcium; via carbonyl oxygen3 Publications
Metal bindingi1061 – 10611Calcium; via carbonyl oxygen3 Publications
Metal bindingi1063 – 10631Calcium3 Publications
Metal bindingi1071 – 10711Iron-sulfur 3 (4Fe-4S)2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

4Fe-4S, Calcium, Iron, Iron-sulfur, Magnesium, Metal-binding, Pyruvate, Thiamine pyrophosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate synthaseCurated (EC:1.2.7.11 Publication)
Alternative name(s):
Pyruvate-ferredoxin oxidoreductase.1 Publication
Short name:
POR1 Publication
Gene namesi
Name:porImported
OrganismiDesulfovibrio africanusImported
Taxonomic identifieri873 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

DrugBankiDB00507. Nitazoxanide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12321232Pyruvate synthasePRO_0000430800Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi1195 ↔ 1212

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.4 Publications

Protein-protein interaction databases

DIPiDIP-29036N.
STRINGi690850.Desaf_2186.

Structurei

Secondary structure

1
1232
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95Combined sources
Helixi10 – 2112Combined sources
Beta strandi23 – 275Combined sources
Turni31 – 333Combined sources
Helixi34 – 4613Combined sources
Beta strandi57 – 604Combined sources
Helixi64 – 7613Combined sources
Beta strandi81 – 855Combined sources
Helixi87 – 10216Combined sources
Beta strandi108 – 1136Combined sources
Beta strandi118 – 1214Combined sources
Helixi128 – 1314Combined sources
Turni132 – 1354Combined sources
Beta strandi139 – 1424Combined sources
Helixi146 – 16318Combined sources
Beta strandi167 – 1726Combined sources
Turni173 – 1786Combined sources
Beta strandi180 – 1845Combined sources
Helixi188 – 1936Combined sources
Helixi197 – 20610Combined sources
Beta strandi215 – 2173Combined sources
Turni222 – 2243Combined sources
Helixi225 – 2306Combined sources
Helixi233 – 25422Combined sources
Beta strandi260 – 2656Combined sources
Beta strandi270 – 2756Combined sources
Helixi279 – 29113Combined sources
Turni292 – 2943Combined sources
Beta strandi297 – 30711Combined sources
Helixi310 – 3156Combined sources
Beta strandi323 – 3308Combined sources
Beta strandi335 – 3373Combined sources
Helixi339 – 35113Combined sources
Beta strandi357 – 3626Combined sources
Helixi365 – 3673Combined sources
Helixi372 – 38312Combined sources
Beta strandi388 – 3914Combined sources
Turni397 – 3993Combined sources
Beta strandi418 – 4258Combined sources
Helixi430 – 44415Combined sources
Beta strandi448 – 4547Combined sources
Beta strandi457 – 4615Combined sources
Beta strandi463 – 47311Combined sources
Beta strandi485 – 4906Combined sources
Helixi492 – 4965Combined sources
Turni500 – 5034Combined sources
Beta strandi509 – 5135Combined sources
Helixi519 – 5257Combined sources
Helixi528 – 5369Combined sources
Beta strandi540 – 5445Combined sources
Helixi546 – 5527Combined sources
Helixi560 – 57011Combined sources
Beta strandi571 – 5744Combined sources
Helixi576 – 58914Combined sources
Helixi595 – 61218Combined sources
Helixi620 – 6245Combined sources
Helixi637 – 6415Combined sources
Helixi643 – 6475Combined sources
Helixi651 – 6533Combined sources
Helixi656 – 6583Combined sources
Helixi669 – 6724Combined sources
Beta strandi679 – 6846Combined sources
Turni686 – 6883Combined sources
Helixi694 – 6985Combined sources
Beta strandi704 – 7096Combined sources
Helixi711 – 7144Combined sources
Helixi729 – 7313Combined sources
Beta strandi735 – 7406Combined sources
Turni742 – 7443Combined sources
Helixi750 – 7545Combined sources
Beta strandi756 – 7594Combined sources
Beta strandi761 – 7666Combined sources
Helixi767 – 7693Combined sources
Helixi771 – 78212Combined sources
Beta strandi789 – 7913Combined sources
Helixi796 – 7994Combined sources
Helixi818 – 82811Combined sources
Helixi829 – 8313Combined sources
Beta strandi832 – 8365Combined sources
Helixi840 – 8467Combined sources
Beta strandi863 – 8653Combined sources
Helixi872 – 89827Combined sources
Turni899 – 9013Combined sources
Helixi904 – 91613Combined sources
Helixi920 – 93314Combined sources
Turni934 – 9363Combined sources
Helixi940 – 9467Combined sources
Helixi947 – 9515Combined sources
Beta strandi956 – 9627Combined sources
Helixi963 – 9675Combined sources
Turni968 – 9703Combined sources
Helixi971 – 9799Combined sources
Beta strandi985 – 9906Combined sources
Beta strandi992 – 9943Combined sources
Turni995 – 9984Combined sources
Helixi1025 – 10306Combined sources
Beta strandi1033 – 10408Combined sources
Turni1042 – 10443Combined sources
Helixi1046 – 105813Combined sources
Beta strandi1059 – 10613Combined sources
Beta strandi1063 – 10686Combined sources
Helixi1072 – 10743Combined sources
Helixi1080 – 10823Combined sources
Helixi1083 – 109210Combined sources
Beta strandi1094 – 10963Combined sources
Beta strandi1099 – 11013Combined sources
Helixi1103 – 11075Combined sources
Beta strandi1112 – 11154Combined sources
Helixi1124 – 11296Combined sources
Helixi1132 – 11409Combined sources
Helixi1142 – 116827Combined sources
Turni1188 – 11914Combined sources
Turni1201 – 12033Combined sources
Beta strandi1215 – 12173Combined sources
Helixi1220 – 122910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B0PX-ray2.31A/B2-1232[»]
1KEKX-ray1.90A/B2-1232[»]
2C3MX-ray1.84A/B2-1232[»]
2C3OX-ray2.70A/B2-1232[»]
2C3PX-ray2.33A/B2-1232[»]
2C3UX-ray2.32A/B2-1232[»]
2C3YX-ray1.93A/B2-1232[»]
2C42X-ray1.78A/B2-1232[»]
2PDAX-ray3.00A/B2-1232[»]
2UZAX-ray2.42A/B2-1232[»]
ProteinModelPortaliP94692.
SMRiP94692. Positions 2-1232.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP94692.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini680 – 709304Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini736 – 767324Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni962 – 9654Thiamine pyrophosphate binding3 Publications
Regioni991 – 9966Thiamine pyrophosphate binding3 Publications

Sequence similaritiesi

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

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
3.40.920.10. 1 hit.
4.10.780.10. 1 hit.
InterProiIPR001450. 4Fe4S-bd_dom.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR019456. Pyrv-flavodox_OxRtase_EKR.
IPR019752. Pyrv/ketoisovalerate_OxRed_cat.
IPR002880. Pyrv_Fd/Flavodoxin_OxRdtase_N.
IPR011895. Pyrv_flavodox_OxRed.
IPR002869. Pyrv_flavodox_OxRed_cen.
IPR029061. THDP-binding.
IPR011766. TPP_enzyme-bd_C.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
[Graphical view]
PfamiPF10371. EKR. 1 hit.
PF00037. Fer4. 1 hit.
PF01558. POR. 1 hit.
PF01855. POR_N. 1 hit.
PF02775. TPP_enzyme_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000159. NifJ. 1 hit.
SMARTiSM00890. EKR. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
SSF53323. SSF53323. 1 hit.
TIGRFAMsiTIGR02176. pyruv_ox_red. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 2 hits.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P94692-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKKMMTTDG NTATAHVAYA MSEVAAIYPI TPSSTMGEEA DDWAAQGRKN
60 70 80 90 100
IFGQTLTIRE MQSEAGAAGA VHGALAAGAL TTTFTASQGL LLMIPNMYKI
110 120 130 140 150
SGELLPGVFH VTARAIAAHA LSIFGDHQDI YAARQTGFAM LASSSVQEAH
160 170 180 190 200
DMALVAHLAA IESNVPFMHF FDGFRTSHEI QKIEVLDYAD MASLVNQKAL
210 220 230 240 250
AEFRAKSMNP EHPHVRGTAQ NPDIYFQGRE AANPYYLKVP GIVAEYMQKV
260 270 280 290 300
ASLTGRSYKL FDYVGAPDAE RVIVSMGSSC ETIEEVINHL AAKGEKIGLI
310 320 330 340 350
KVRLYRPFVS EAFFAALPAS AKVITVLDRT KEPGAPGDPL YLDVCSAFVE
360 370 380 390 400
RGEAMPKILA GRYGLGSKEF SPAMVKSVYD NMSGAKKNHF TVGIEDDVTG
410 420 430 440 450
TSLPVDNAFA DTTPKGTIQC QFWGLGADGT VGANKQAIKI IGDNTDLFAQ
460 470 480 490 500
GYFSYDSKKS GGITISHLRF GEKPIQSTYL VNRADYVACH NPAYVGIYDI
510 520 530 540 550
LEGIKDGGTF VLNSPWSSLE DMDKHLPSGI KRTIANKKLK FYNIDAVKIA
560 570 580 590 600
TDVGLGGRIN MIMQTAFFKL AGVLPFEKAV DLLKKSIHKA YGKKGEKIVK
610 620 630 640 650
MNTDAVDQAV TSLQEFKYPD SWKDAPAETK AEPMTNEFFK NVVKPILTQQ
660 670 680 690 700
GDKLPVSAFE ADGRFPLGTS QFEKRGVAIN VPQWVPENCI QCNQCAFVCP
710 720 730 740 750
HSAILPVLAK EEELVGAPAN FTALEAKGKE LKGYKFRIQI NTLDCMGCGN
760 770 780 790 800
CADICPPKEK ALVMQPLDTQ RDAQVPNLEY AARIPVKSEV LPRDSLKGSQ
810 820 830 840 850
FQEPLMEFSG ACSGCGETPY VRVITQLFGE RMFIANATGC SSIWGASAPS
860 870 880 890 900
MPYKTNRLGQ GPAWGNSLFE DAAEYGFGMN MSMFARRTHL ADLAAKALES
910 920 930 940 950
DASGDVKEAL QGWLAGKNDP IKSKEYGDKL KKLLAGQKDG LLGQIAAMSD
960 970 980 990 1000
LYTKKSVWIF GGDGWAYDIG YGGLDHVLAS GEDVNVFVMD TEVYSNTGGQ
1010 1020 1030 1040 1050
SSKATPTGAV AKFAAAGKRT GKKDLARMVM TYGYVYVATV SMGYSKQQFL
1060 1070 1080 1090 1100
KVLKEAESFP GPSLVIAYAT CINQGLRKGM GKSQDVMNTA VKSGYWPLFR
1110 1120 1130 1140 1150
YDPRLAAQGK NPFQLDSKAP DGSVEEFLMA QNRFAVLDRS FPEDAKRLRA
1160 1170 1180 1190 1200
QVAHELDVRF KELEHMAATN IFESFAPAGG KADGSVDFGE GAEFCTRDDT
1210 1220 1230
PMMARPDSGE ACDQNRAGTS EQQGDLSKRT KK
Length:1,232
Mass (Da):133,680
Last modified:May 1, 1997 - v1
Checksum:i55D84F536CCFFDBF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09702 Genomic DNA. Translation: CAA70873.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09702 Genomic DNA. Translation: CAA70873.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B0PX-ray2.31A/B2-1232[»]
1KEKX-ray1.90A/B2-1232[»]
2C3MX-ray1.84A/B2-1232[»]
2C3OX-ray2.70A/B2-1232[»]
2C3PX-ray2.33A/B2-1232[»]
2C3UX-ray2.32A/B2-1232[»]
2C3YX-ray1.93A/B2-1232[»]
2C42X-ray1.78A/B2-1232[»]
2PDAX-ray3.00A/B2-1232[»]
2UZAX-ray2.42A/B2-1232[»]
ProteinModelPortaliP94692.
SMRiP94692. Positions 2-1232.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29036N.
STRINGi690850.Desaf_2186.

Chemistry

DrugBankiDB00507. Nitazoxanide.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP94692.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
3.40.920.10. 1 hit.
4.10.780.10. 1 hit.
InterProiIPR001450. 4Fe4S-bd_dom.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR019456. Pyrv-flavodox_OxRtase_EKR.
IPR019752. Pyrv/ketoisovalerate_OxRed_cat.
IPR002880. Pyrv_Fd/Flavodoxin_OxRdtase_N.
IPR011895. Pyrv_flavodox_OxRed.
IPR002869. Pyrv_flavodox_OxRed_cen.
IPR029061. THDP-binding.
IPR011766. TPP_enzyme-bd_C.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
[Graphical view]
PfamiPF10371. EKR. 1 hit.
PF00037. Fer4. 1 hit.
PF01558. POR. 1 hit.
PF01855. POR_N. 1 hit.
PF02775. TPP_enzyme_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000159. NifJ. 1 hit.
SMARTiSM00890. EKR. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
SSF53323. SSF53323. 1 hit.
TIGRFAMsiTIGR02176. pyruv_ox_red. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 2 hits.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Isolation and analysis of the gene encoding the pyruvate-ferredoxin oxidoreductase of Desulfovibrio africanus, production of the recombinant enzyme in Escherichia coli, and effect of carboxy-terminal deletions on its stability."
    Pieulle L., Magro V., Hatchikian E.C.
    J. Bacteriol. 179:5684-5692(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-18; 304-313; 484-504 AND 1198-1216, FUNCTION.
    Strain: ATCC 19996 / DSM 2603 / NCIB 8401 / Benghazi.
  2. "Isolation and characterization of the pyruvate-ferredoxin oxidoreductase from the sulfate-reducing bacterium Desulfovibrio africanus."
    Pieulle L., Guigliarelli B., Asso M., Dole F., Bernadac A., Hatchikian E.C.
    Biochim. Biophys. Acta 1250:49-59(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: ATCC 19996 / DSM 2603 / NCIB 8401 / Benghazi.
  3. "Crystal structures of the key anaerobic enzyme pyruvate:ferredoxin oxidoreductase, free and in complex with pyruvate."
    Chabriere E., Charon M.H., Volbeda A., Pieulle L., Hatchikian E.C., Fontecilla-Camps J.C.
    Nat. Struct. Biol. 6:182-190(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 2-1232 IN COMPLEX WITH IRON-SULFUR(4FE-4S); CALCIUM ION; MAGNESIUM ION; PYRUVATE AND THIAMINEPYROPHOSPHATE, SUBUNIT, DISULFIDE BOND.
  4. "Crystal structure of the free radical intermediate of pyruvate:ferredoxin oxidoreductase."
    Chabriere E., Vernede X., Guigliarelli B., Charon M.H., Hatchikian E.C., Fontecilla-Camps J.C.
    Science 294:2559-2563(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-1232 IN COMPLEX WITH CALCIUM; IRON-SULFUR(4FE-4S); MAGNESIUM AND THIAMINEPYROPHOSPHATE ANALOG, SUBUNIT.
  5. "Flexibility of thiamine diphosphate revealed by kinetic crystallographic studies of the reaction of pyruvate-ferredoxin oxidoreductase with pyruvate."
    Cavazza C., Contreras-Martel C., Pieulle L., Chabriere E., Hatchikian E.C., Fontecilla-Camps J.C.
    Structure 14:217-224(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 2-1232 IN COMPLEX WITH IRON-SULFUR(4FE-4S); CALCIUM ION; MAGNESIUM ION; PYRUVATE AND THIAMINEPYROPHOSPHATE, SUBUNIT.

Entry informationi

Entry nameiPOR_DESAF
AccessioniPrimary (citable) accession number: P94692
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 29, 2014
Last sequence update: May 1, 1997
Last modified: June 24, 2015
This is version 102 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

External Data

Dasty 3

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 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.