Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Binding sitei31Pyruvate2 Publications1
Sitei31Important for catalytic activity1 Publication1
Binding sitei64Thiamine pyrophosphate2 Publications1
Sitei64Important for catalytic activity1 Publication1
Binding sitei114Pyruvate2 Publications1
Sitei114Important for catalytic activity1 Publication1
Metal bindingi689Iron-sulfur 1 (4Fe-4S)3 Publications1
Metal bindingi692Iron-sulfur 1 (4Fe-4S)3 Publications1
Metal bindingi695Iron-sulfur 1 (4Fe-4S)3 Publications1
Metal bindingi699Iron-sulfur 2 (4Fe-4S)3 Publications1
Metal bindingi745Iron-sulfur 2 (4Fe-4S)3 Publications1
Metal bindingi748Iron-sulfur 2 (4Fe-4S)3 Publications1
Metal bindingi751Iron-sulfur 2 (4Fe-4S)3 Publications1
Metal bindingi755Iron-sulfur 1 (4Fe-4S)3 Publications1
Metal bindingi812Iron-sulfur 3 (4Fe-4S)3 Publications1
Metal bindingi815Iron-sulfur 3 (4Fe-4S)3 Publications1
Binding sitei817Thiamine pyrophosphate3 Publications1
Metal bindingi840Iron-sulfur 3 (4Fe-4S)3 Publications1
Binding sitei840Thiamine pyrophosphate3 Publications1
Metal bindingi963Magnesium3 Publications1
Metal bindingi983Calcium3 Publications1
Metal bindingi985Calcium3 Publications1
Metal bindingi991Magnesium3 Publications1
Metal bindingi993Magnesium; via carbonyl oxygen3 Publications1
Sitei996Important for catalytic activity1 Publication1
Metal bindingi1056Calcium; via carbonyl oxygen3 Publications1
Metal bindingi1059Calcium; via carbonyl oxygen3 Publications1
Metal bindingi1061Calcium; via carbonyl oxygen3 Publications1
Metal bindingi1063Calcium3 Publications1
Metal bindingi1071Iron-sulfur 3 (4Fe-4S)2 Publications1

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 oxidoreductase1 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 databases

DrugBankiDB00507. Nitazoxanide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004308001 – 1232Pyruvate synthaseAdd BLAST1232

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

11232
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 9Combined sources5
Helixi10 – 21Combined sources12
Beta strandi23 – 27Combined sources5
Turni31 – 33Combined sources3
Helixi34 – 46Combined sources13
Beta strandi57 – 60Combined sources4
Helixi64 – 76Combined sources13
Beta strandi81 – 85Combined sources5
Helixi87 – 102Combined sources16
Beta strandi108 – 113Combined sources6
Beta strandi118 – 121Combined sources4
Helixi128 – 131Combined sources4
Turni132 – 135Combined sources4
Beta strandi139 – 142Combined sources4
Helixi146 – 163Combined sources18
Beta strandi167 – 172Combined sources6
Turni173 – 178Combined sources6
Beta strandi180 – 184Combined sources5
Helixi188 – 193Combined sources6
Helixi197 – 206Combined sources10
Beta strandi215 – 217Combined sources3
Turni222 – 224Combined sources3
Helixi225 – 230Combined sources6
Helixi233 – 254Combined sources22
Beta strandi260 – 265Combined sources6
Beta strandi270 – 275Combined sources6
Helixi279 – 291Combined sources13
Turni292 – 294Combined sources3
Beta strandi297 – 307Combined sources11
Helixi310 – 315Combined sources6
Beta strandi323 – 330Combined sources8
Beta strandi335 – 337Combined sources3
Helixi339 – 351Combined sources13
Beta strandi357 – 362Combined sources6
Helixi365 – 367Combined sources3
Helixi372 – 383Combined sources12
Beta strandi388 – 391Combined sources4
Turni397 – 399Combined sources3
Beta strandi418 – 425Combined sources8
Helixi430 – 444Combined sources15
Beta strandi448 – 454Combined sources7
Beta strandi457 – 461Combined sources5
Beta strandi463 – 473Combined sources11
Beta strandi485 – 490Combined sources6
Helixi492 – 496Combined sources5
Turni500 – 503Combined sources4
Beta strandi509 – 513Combined sources5
Helixi519 – 525Combined sources7
Helixi528 – 536Combined sources9
Beta strandi540 – 544Combined sources5
Helixi546 – 552Combined sources7
Helixi560 – 570Combined sources11
Beta strandi571 – 574Combined sources4
Helixi576 – 589Combined sources14
Helixi595 – 612Combined sources18
Helixi620 – 624Combined sources5
Helixi637 – 641Combined sources5
Helixi643 – 647Combined sources5
Helixi651 – 653Combined sources3
Helixi656 – 658Combined sources3
Helixi669 – 672Combined sources4
Beta strandi679 – 684Combined sources6
Turni686 – 688Combined sources3
Helixi694 – 698Combined sources5
Beta strandi704 – 709Combined sources6
Helixi711 – 714Combined sources4
Helixi729 – 731Combined sources3
Beta strandi735 – 740Combined sources6
Turni742 – 744Combined sources3
Helixi750 – 754Combined sources5
Beta strandi756 – 759Combined sources4
Beta strandi761 – 766Combined sources6
Helixi767 – 769Combined sources3
Helixi771 – 782Combined sources12
Beta strandi789 – 791Combined sources3
Helixi796 – 799Combined sources4
Helixi818 – 828Combined sources11
Helixi829 – 831Combined sources3
Beta strandi832 – 836Combined sources5
Helixi840 – 846Combined sources7
Beta strandi863 – 865Combined sources3
Helixi872 – 898Combined sources27
Turni899 – 901Combined sources3
Helixi904 – 916Combined sources13
Helixi920 – 933Combined sources14
Turni934 – 936Combined sources3
Helixi940 – 946Combined sources7
Helixi947 – 951Combined sources5
Beta strandi956 – 962Combined sources7
Helixi963 – 967Combined sources5
Turni968 – 970Combined sources3
Helixi971 – 979Combined sources9
Beta strandi985 – 990Combined sources6
Beta strandi992 – 994Combined sources3
Turni995 – 998Combined sources4
Helixi1025 – 1030Combined sources6
Beta strandi1033 – 1040Combined sources8
Turni1042 – 1044Combined sources3
Helixi1046 – 1058Combined sources13
Beta strandi1059 – 1061Combined sources3
Beta strandi1063 – 1068Combined sources6
Helixi1072 – 1074Combined sources3
Helixi1080 – 1082Combined sources3
Helixi1083 – 1092Combined sources10
Beta strandi1094 – 1096Combined sources3
Beta strandi1099 – 1101Combined sources3
Helixi1103 – 1107Combined sources5
Beta strandi1112 – 1115Combined sources4
Helixi1124 – 1129Combined sources6
Helixi1132 – 1140Combined sources9
Helixi1142 – 1168Combined sources27
Turni1188 – 1191Combined sources4
Turni1201 – 1203Combined sources3
Beta strandi1215 – 1217Combined sources3
Helixi1220 – 1229Combined sources10

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP94692.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini680 – 7094Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd BLAST30
Domaini736 – 7674Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd BLAST32

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni962 – 965Thiamine pyrophosphate binding3 Publications4
Regioni991 – 996Thiamine pyrophosphate binding3 Publications6

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105D95. Bacteria.
COG0674. LUCA.
COG1013. LUCA.
COG1014. LUCA.

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.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR033412. PFOR_II.
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/PFOR_II.
[Graphical view]
PfamiPF10371. EKR. 1 hit.
PF17147. PFOR_II. 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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29036N.
STRINGi690850.Desaf_2186.

Chemistry databases

DrugBankiDB00507. Nitazoxanide.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105D95. Bacteria.
COG0674. LUCA.
COG1013. LUCA.
COG1014. LUCA.

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.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR033412. PFOR_II.
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/PFOR_II.
[Graphical view]
PfamiPF10371. EKR. 1 hit.
PF17147. PFOR_II. 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...

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: November 2, 2016
This is version 110 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.