Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 107 (22 Apr 2020)
Sequence version 1 (24 Jan 2006)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Pyruvate:ferredoxin oxidoreductase

Gene

Moth_0064

Organism
Moorella thermoacetica (strain ATCC 39073 / JCM 9320)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA and carbon dioxide. The two electrons that are generated as a result of pyruvate decarboxylation are used in the reduction of low potential ferredoxins, which provide reducing equivalents for central metabolism. Also catalyzes the reverse reaction, i.e. the synthesis of pyruvate from acetyl-CoA and carbon dioxide. Appears to function physiologically in both directions (PubMed:10878009). The oxidation of pyruvate by PFOR is required to connect glycolysis and the Wood-Ljungdahl pathway of reductive acetogenesis. The conversion of acetyl-CoA to pyruvate links the Wood-Ljungdahl pathway of autotrophic CO2 fixation to the reductive tricarboxylic acid cycle (PubMed:10878009, PubMed:29581263). Can use methyl viologen as electron carrier in vitro (PubMed:9214293, PubMed:29581263).2 Publications3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 3.2 sec(-1) for the synthesis of pyruvate from acetyl-CoA and CO2 with methyl viologen as electron donor (PubMed:10878009). kcat is 2.0 sec(-1) for the synthesis of pyruvate from acetyl-CoA and CO2 with reduced ferredoxin as electron donor (PubMed:10878009). kcat is 28 sec(-1) for the oxidative decarboxylation of pyruvate with methyl viologen as electron acceptor (PubMed:10878009). kcat is 33 sec(-1) for the oxidative decarboxylation of pyruvate with methyl viologen as electron acceptor (PubMed:29581263). kcat is 29.6 sec(-1) for the oxidative decarboxylation of pyruvate with oxidized ferredoxin as electron acceptor (PubMed:10878009). kcat is 19.8 sec(-1) for the oxidative decarboxylation of pyruvate with oxidized rubredoxin as electron acceptor (PubMed:10878009).2 Publications
  1. KM=9 µM for acetyl-CoA1 Publication
  2. KM=2.0 mM for CO21 Publication
  3. KM=0.30 mM for pyruvate1 Publication
  4. KM=0.32 µM for oxidized ferredoxin1 Publication
  5. KM=0.27 µM for reduced ferredoxin1 Publication
  6. KM=9.4 µM for oxidized rubredoxin1 Publication
  7. KM=1.1 mM for methyl viologen (in the oxidative decarboxylation of pyruvate)1 Publication
  1. Vmax=1.6 µmol/min/mg enzyme for the synthesis of pyruvate from acetyl-CoA and CO2 with methyl viologen as electron donor1 Publication
  2. Vmax=1.0 µmol/min/mg enzyme for the synthesis of pyruvate with reduced ferredoxin as electron donor1 Publication
  3. Vmax=14.2 µmol/min/mg enzyme for the oxidative decarboxylation of pyruvate with methyl viologen as electron acceptor1 Publication
  4. Vmax=14.8 µmol/min/mg enzyme for the oxidative decarboxylation of pyruvate with oxidized ferredoxin as electron acceptor1 Publication
  5. Vmax=9.9 µmol/min/mg enzyme for the oxidative decarboxylation of pyruvate with oxidized rubredoxin as electron acceptor1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei29Pyruvate1 PublicationImported1
Binding sitei112Pyruvate1 PublicationImported1
Binding sitei456CoA; via carbonyl oxygen1 PublicationImported1
Binding sitei556CoA1 PublicationImported1
Binding sitei598CoA1 PublicationImported1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi686Iron-sulfur 1 (4Fe-4S)1 PublicationImported1
Metal bindingi689Iron-sulfur 1 (4Fe-4S)1 PublicationImported1
Metal bindingi692Iron-sulfur 1 (4Fe-4S)1 PublicationImported1
Metal bindingi696Iron-sulfur 2 (4Fe-4S)1 PublicationImported1
Metal bindingi742Iron-sulfur 2 (4Fe-4S)1 PublicationImported1
Metal bindingi745Iron-sulfur 2 (4Fe-4S)1 PublicationImported1
Metal bindingi748Iron-sulfur 2 (4Fe-4S)1 PublicationImported1
Metal bindingi752Iron-sulfur 1 (4Fe-4S)1 PublicationImported1
Metal bindingi809Iron-sulfur 3 (4Fe-4S)1 PublicationImported1
Metal bindingi812Iron-sulfur 3 (4Fe-4S)1 PublicationImported1
Binding sitei814Thiamine pyrophosphate1 PublicationImported1
Metal bindingi837Iron-sulfur 3 (4Fe-4S)1 PublicationImported1
Binding sitei837Thiamine pyrophosphate; via amide nitrogen1 PublicationImported1
Metal bindingi967Magnesium1 PublicationImported1
Metal bindingi995Magnesium1 PublicationImported1
Metal bindingi997Magnesium; via carbonyl oxygen1 PublicationImported1
Binding sitei1000Pyruvate1 PublicationImported1
Metal bindingi1075Iron-sulfur 3 (4Fe-4S)1 PublicationImported1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Transport
Ligand4Fe-4S, Iron, Iron-sulfur, Magnesium, Metal-binding, Pyruvate

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MTHE264732:G1G5J-72-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Pyruvate:ferredoxin oxidoreductase1 Publication (EC:1.2.7.11 Publication1 Publication)
Short name:
PFOR1 Publication
Alternative name(s):
Pyruvate synthase1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Ordered Locus Names:Moth_0064Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMoorella thermoacetica (strain ATCC 39073 / JCM 9320)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri264732 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeMoorella groupMoorella
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000007053 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004462631 – 1171Pyruvate:ferredoxin oxidoreductaseAdd BLAST1171

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
264732.Moth_0064

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11171
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q2RMD6

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini677 – 7064Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd BLAST30
Domaini733 – 7644Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd BLAST32

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni424 – 428CoA binding1 PublicationImported5
Regioni967 – 969Thiamine pyrophosphate binding1 PublicationImported3
Regioni995 – 1000Thiamine pyrophosphate binding1 PublicationImported6

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105D95 Bacteria
COG0674 LUCA
COG1013 LUCA
COG1014 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_002569_0_0_9

KEGG Orthology (KO)

More...
KOi
K03737

Identification of Orthologs from Complete Genome Data

More...
OMAi
NTVMQVC

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.920, 1 hit
3.40.920.10, 1 hit
4.10.780.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR017896 4Fe4S_Fe-S-bd
IPR017900 4Fe4S_Fe_S_CS
IPR033412 PFOR_II
IPR037112 Pyrv-flavodox_OxR_EKR_sf
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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF10371 EKR, 1 hit
PF17147 PFOR_II, 1 hit
PF01558 POR, 1 hit
PF01855 POR_N, 1 hit
PF02775 TPP_enzyme_C, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000159 NifJ, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00890 EKR, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52518 SSF52518, 2 hits
SSF52922 SSF52922, 1 hit
SSF53323 SSF53323, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02176 pyruv_ox_red, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00198 4FE4S_FER_1, 2 hits
PS51379 4FE4S_FER_2, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q2RMD6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPKQTLDGNT AAAHVAYAMS EVATIYPITP SSPMAEIADE WAAHGRKNIF
60 70 80 90 100
GKTLQVAEMQ SEAGAAGAVH GSLAAGALTT TFTASQGLLL MIPNMYKIAG
110 120 130 140 150
ELLPCVFHVA ARALSTHALS IFGDHADVMA ARQTGFAMLS SASVQEVMDL
160 170 180 190 200
ALVAHLATLK ARVPFVHFFD GFRTSHEVQK IDVIEYEDMA KLVDWDAIRA
210 220 230 240 250
FRQRALNPEH PHQRGTAQNP DIYFQSREAA NPYYLATPGI VAQVMEQVAG
260 270 280 290 300
LTGRHYHLFD YAGAPDAERV IVSMGSSCEV IEETVNYLVE KGEKVGLIKV
310 320 330 340 350
RLFRPFSAEH FLKVLPASVK RIAVLDRTKE PGSLGEPLYE DVQTVLAEHG
360 370 380 390 400
KNILVVGGRY GLGSKEFNPS MVKAVFDNLA ATTPKNKFTV GITDDVTHTS
410 420 430 440 450
LEIKEHIDTS PKGTFRCKFF GLGSDGTVGA NKNSIKIIGD HTDMYAQGYF
460 470 480 490 500
VYDSKKSGGV TISHLRFGKQ PIQSAYLIDQ ADLIACHNPS YVGRYNLLEG
510 520 530 540 550
IKPGGIFLLN STWSAEEMDS RLPADMKRTI ATKKLKFYNI DAVKIAQEIG
560 570 580 590 600
LGSRINVIMQ TAFFKIANVI PVDEAIKYIK DSIVKTYGKK GDKILNMNFA
610 620 630 640 650
AVDRALEALE EIKYPASWAD AVDEAAATVT EEPEFIQKVL RPINALKGDE
660 670 680 690 700
LPVSTFTPDG VFPVGTTKYE KRGIAVNIPQ WQPENCIQCN QCSLVCPHAA
710 720 730 740 750
IRPYLAKPAD LAGAPETFVT KDAIGKEAAG LKFRIQVSPL DCTGCGNCAD
760 770 780 790 800
VCPAKVKALT MVPLEEVTAV EEANYNFAEQ LPEVKVNFNP ATVKGSQFRQ
810 820 830 840 850
PLLEFSGACA GCGETPYVKL VTQLFGDRMI IANATGCSSI WGGSAPACPY
860 870 880 890 900
TVNRQGHGPA WASSLFEDNA EFGYGMALAV AKRQDELATA ISKALEAPVS
910 920 930 940 950
AAFKAACEGW LAGKDDADRS REYGDRIKAL LPGEISQASG EVKDLLLDID
960 970 980 990 1000
RQKDYLTKKS IWIIGGDGWA YDIGYGGLDH VLASGANVNV LVLDTEVYSN
1010 1020 1030 1040 1050
TGGQSSKATQ TGAVARFAAG GKFTKKKDLG LMAMSYGYVY VASVAMGASH
1060 1070 1080 1090 1100
SQLMKALIEA EKYDGPSLII AYAPCINHGI NMTYSQREAK KAVEAGYWPL
1110 1120 1130 1140 1150
YRYNPQLAQE GKNPFILDYK TPTASFRDFL MGEIRYTSLK KQFPEKAEQL
1160 1170
FAKAEADAKA RLEQYKKLAE G
Length:1,171
Mass (Da):127,277
Last modified:January 24, 2006 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i3F171E506F8D9B6E
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
CP000232 Genomic DNA Translation: ABC18403.1

NCBI Reference Sequences

More...
RefSeqi
WP_011391612.1, NC_007644.1
YP_428946.1, NC_007644.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
ABC18403; ABC18403; Moth_0064

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3830814

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mta:Moth_0064

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|264732.11.peg.68

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000232 Genomic DNA Translation: ABC18403.1
RefSeqiWP_011391612.1, NC_007644.1
YP_428946.1, NC_007644.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6CINX-ray2.60A/B/C/D/E/F1-1171[»]
6CIOX-ray3.00A/B/C/D/E/F1-1171[»]
6CIPX-ray3.19A/B/C/D/E/F1-1171[»]
6CIQX-ray3.30A/B/C1-1171[»]
SMRiQ2RMD6
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi264732.Moth_0064

Genome annotation databases

EnsemblBacteriaiABC18403; ABC18403; Moth_0064
GeneIDi3830814
KEGGimta:Moth_0064
PATRICifig|264732.11.peg.68

Phylogenomic databases

eggNOGiENOG4105D95 Bacteria
COG0674 LUCA
COG1013 LUCA
COG1014 LUCA
HOGENOMiCLU_002569_0_0_9
KOiK03737
OMAiNTVMQVC

Enzyme and pathway databases

BioCyciMTHE264732:G1G5J-72-MONOMER

Family and domain databases

Gene3Di3.40.50.920, 1 hit
3.40.920.10, 1 hit
4.10.780.10, 1 hit
InterProiView protein in InterPro
IPR017896 4Fe4S_Fe-S-bd
IPR017900 4Fe4S_Fe_S_CS
IPR033412 PFOR_II
IPR037112 Pyrv-flavodox_OxR_EKR_sf
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
PfamiView protein in Pfam
PF10371 EKR, 1 hit
PF17147 PFOR_II, 1 hit
PF01558 POR, 1 hit
PF01855 POR_N, 1 hit
PF02775 TPP_enzyme_C, 1 hit
PIRSFiPIRSF000159 NifJ, 1 hit
SMARTiView protein in SMART
SM00890 EKR, 1 hit
SUPFAMiSSF52518 SSF52518, 2 hits
SSF52922 SSF52922, 1 hit
SSF53323 SSF53323, 1 hit
TIGRFAMsiTIGR02176 pyruv_ox_red, 1 hit
PROSITEiView protein in PROSITE
PS00198 4FE4S_FER_1, 2 hits
PS51379 4FE4S_FER_2, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPFOR_MOOTA
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q2RMD6
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 13, 2019
Last sequence update: January 24, 2006
Last modified: April 22, 2020
This is version 107 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again