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
Submitted name:

Coenzyme A disulfide reductase

Gene

ygbD

Organism
Bacillus anthracis
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381Coenzyme ACombined sources
Binding sitei42 – 421Coenzyme ACombined sources
Binding sitei61 – 611Coenzyme ACombined sources
Binding sitei80 – 801FAD; via amide nitrogen and carbonyl oxygenCombined sources
Binding sitei187 – 1871NADPCombined sources
Binding sitei243 – 2431NAD; via amide nitrogenCombined sources
Binding sitei243 – 2431NADP; via amide nitrogenCombined sources
Binding sitei282 – 2821FADCombined sources
Binding sitei298 – 2981NAD; via carbonyl oxygenCombined sources
Binding sitei298 – 2981NADP; via carbonyl oxygenCombined sources
Binding sitei304 – 3041Coenzyme ACombined sources
Binding sitei308 – 3081Coenzyme ACombined sources
Binding sitei329 – 3291NAD; via carbonyl oxygenCombined sources
Binding sitei329 – 3291NADP; via carbonyl oxygenCombined sources
Binding sitei425 – 4251FAD; via carbonyl oxygenCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 113FADCombined sources
Nucleotide bindingi32 – 332FADCombined sources
Nucleotide bindingi41 – 422FADCombined sources
Nucleotide bindingi160 – 1645NADCombined sources
Nucleotide bindingi160 – 1645NADPCombined sources
Nucleotide bindingi180 – 1823NADCombined sources
Nucleotide bindingi180 – 1823NADPCombined sources
Nucleotide bindingi300 – 3012FADCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

FADCombined sources, Flavoprotein, NADCombined sources, NADPCombined sources, Nucleotide-bindingCombined sources

Enzyme and pathway databases

BioCyciBANT260799:GJAJ-1244-MONOMER.
BANT261594:GJ7F-1300-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
Coenzyme A disulfide reductaseImported
Submitted name:
Pyridine nucleotide-disulfide oxidoreductase, class IImported
Gene namesi
Name:ygbDImported
Ordered Locus Names:GBAA_1263Imported
ORF Names:BASH2_04592Imported
OrganismiBacillus anthracisImported
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000000594 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi198094.BA_1263.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CGBX-ray1.90A/B2-444[»]
3CGCX-ray2.30A/B1-444[»]
3CGDX-ray2.25A/B1-444[»]
3CGEX-ray2.26A/B1-444[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 293292FAD/NAD-binding_domInterPro annotationAdd
BLAST
Domaini330 – 430101Pyr_redox_dimInterPro annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni18 – 214Coenzyme A bindingCombined sources
Regioni441 – 4422Coenzyme A bindingCombined sources

Phylogenomic databases

eggNOGiENOG4107QMW. Bacteria.
COG0446. LUCA.
HOGENOMiHOG000276710.
OMAiPVWHPLI.
OrthoDBiEOG6QVRCJ.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.

Sequencei

Sequence statusi: Complete.

Q81TK8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNYVIIGGDA AGMSAAMQIV RNDENANVVT LEKGEIYSYA QCGLPYVISG
60 70 80 90 100
AIASTEKLIA RNVKTFRDKY GIDAKVRHEV TKVDTEKKIV YAEHTKTKDV
110 120 130 140 150
FEFSYDRLLI ATGVRPVMPE WEGRDLQGVH LLKTIPDAER ILKTLETNKV
160 170 180 190 200
EDVTIIGGGA IGLEMAETFV ELGKKVRMIE RNDHIGTIYD GDMAEYIYKE
210 220 230 240 250
ADKHHIEILT NENVKAFKGN ERVEAVETDK GTYKADLVLV SVGVKPNTDF
260 270 280 290 300
LEGTNIRTNH KGAIEVNAYM QTNVQDVYAA GDCATHYHVI KEIHDHIPIG
310 320 330 340 350
TTANKQGRLA GLNMLDKRRA FKGTLGTGII KFMNLTLART GLNEKEAKGL
360 370 380 390 400
HIPYKTVKVD STNMAGYYPN AKPLYLKLLY RSDTKQLLGG QVIGEEGVDK
410 420 430 440
RIDVIAMALF NKMSIHDLED VDLSYAPPYN SVWDPIQQAA RRAE
Length:444
Mass (Da):49,483
Last modified:June 1, 2003 - v1
Checksum:i065E3692E48ECFDA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017334 Genomic DNA. Translation: AAT30354.2.
AP014833 Genomic DNA. Translation: BAR77999.1.
RefSeqiWP_001110220.1. NZ_LHUO01000014.1.

Genome annotation databases

EnsemblBacteriaiAAT30354; AAT30354; GBAA_1263.
KOM63931; KOM63931; AB168_02905.
KOM64780; KOM64780; AB166_26535.
KOM70870; KOM70870; AB165_23625.
KOM78584; KOM78584; AB167_12390.
KOM84581; KOM84581; AB164_10155.
KOM91356; KOM91356; AB169_20060.
KON04514; KON04514; AB170_18730.
KON16112; KON16112; AB171_21450.
KON24294; KON24294; AB163_10310.
KOR62307; KOR62307; ADT21_06215.
KOR66674; KOR66674; ADT20_17215.
KEGGibanh:HYU01_06465.
bar:GBAA_1263.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017334 Genomic DNA. Translation: AAT30354.2.
AP014833 Genomic DNA. Translation: BAR77999.1.
RefSeqiWP_001110220.1. NZ_LHUO01000014.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CGBX-ray1.90A/B2-444[»]
3CGCX-ray2.30A/B1-444[»]
3CGDX-ray2.25A/B1-444[»]
3CGEX-ray2.26A/B1-444[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198094.BA_1263.

Protocols and materials databases

DNASUi1087666.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT30354; AAT30354; GBAA_1263.
KOM63931; KOM63931; AB168_02905.
KOM64780; KOM64780; AB166_26535.
KOM70870; KOM70870; AB165_23625.
KOM78584; KOM78584; AB167_12390.
KOM84581; KOM84581; AB164_10155.
KOM91356; KOM91356; AB169_20060.
KON04514; KON04514; AB170_18730.
KON16112; KON16112; AB171_21450.
KON24294; KON24294; AB163_10310.
KOR62307; KOR62307; ADT21_06215.
KOR66674; KOR66674; ADT20_17215.
KEGGibanh:HYU01_06465.
bar:GBAA_1263.

Phylogenomic databases

eggNOGiENOG4107QMW. Bacteria.
COG0446. LUCA.
HOGENOMiHOG000276710.
OMAiPVWHPLI.
OrthoDBiEOG6QVRCJ.

Enzyme and pathway databases

BioCyciBANT260799:GJAJ-1244-MONOMER.
BANT261594:GJ7F-1300-MONOMER.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: a structural analysis of dual NAD(P)H specificity."
    Wallen J.R., Paige C., Mallett T.C., Karplus P.A., Claiborne A.
    Biochemistry 47:5182-5193(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-444 IN COMPLEX WITH COENZYME A; FAD; NAD AND NADP.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames ancestorImported and Ames AncestorImported.
  3. "Bacillus anthracis whole genome sequence."
    Okutani A., Morikawa S., Inoue S.
    Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Shikan-NIIDImported.

Entry informationi

Entry nameiQ81TK8_BACAN
AccessioniPrimary (citable) accession number: Q81TK8
Secondary accession number(s): E9R6F6
, E9R6F7, Q6I1U0, Q6KVN0
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: July 6, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.