Fumarate reductase iron-sulfur subunit - Mycobacterium tuberculosis

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Q10761 (FRDB_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 88. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Fumarate reductase iron-sulfur subunit
EC=1.3.99.1

Gene names

Name:	frdB
Ordered Locus Names:	Rv1553, MT1604
ORF Names:	MTCY48.12c

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	247 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Succinate + acceptor = fumarate + reduced acceptor.
Cofactor	Binds 1 2Fe-2S cluster By similarity. Binds 1 3Fe-4S cluster By similarity. Binds 1 4Fe-4S cluster By similarity.
Subunit structure	Fumarate dehydrogenase forms part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur, and two hydrophobic anchor proteins By similarity.
Sequence similarities	Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 4Fe-4S ferredoxin-type domain.

Ontologies

Keywords
Biological process	Electron transport Transport Tricarboxylic acid cycle
Ligand	2Fe-2S 3Fe-4S 4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW succinate dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 247

247

Fumarate reductase iron-sulfur subunit

PRO_0000158705

Regions

Domain

14 – 94

2Fe-2S ferredoxin-type

Domain

140 – 169

4Fe-4S ferredoxin-type

Sites

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

149

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

152

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

155

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

159

Iron-sulfur 3 (3Fe-4S) By similarity

Metal binding

205

Iron-sulfur 3 (3Fe-4S) By similarity

Metal binding

211

Iron-sulfur 3 (3Fe-4S) By similarity

Metal binding

215

Iron-sulfur 2 (4Fe-4S) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q10761 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 15863DCCB2C82B0B
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FASTA

247

27,234

        10         20         30         40         50         60 
MMDRIVMEVS RYRPEIESAP TFQAYEVPLT REWAVLDGLT YIKDHLDGTL SFRWSCRMGI 

        70         80         90        100        110        120 
CGSSGMTING DPKLACATFL ADYLPGPVRV EPMRNFPVIR DLVVDISDFM AKLPSVKPWL 

       130        140        150        160        170        180 
VRHDEPPVED GEYRQTPAEL DAFKQFSMCI NCMLCYSACP VYALDPDFLG PAAIALGQRY 

       190        200        210        220        230        240 
NLDSRDQGAA DRRDVLAAAD GAWACTLVGE CSTACPKGVD PAGAIQRYKL TAATHALKKL 


LFPWGGG

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References

[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842577 Genomic DNA. Translation: CAA98310.1. AE000516 Genomic DNA. Translation: AAK45871.1.
PIR	F70762.
RefSeq	NP_216069.1. NC_000962.2. NP_336057.1. NC_002755.2.
3D structure databases
ProteinModelPortal	Q10761.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000000779; EBMYCP00000000779; EBMYCG00000000779. EBMYCT00000069542; EBMYCP00000067601; EBMYCG00000069537.
GeneID	886378. 924333.
GenomeReviews	Gene locus MT1604 in contig AE000516_GR. Gene locus Rv1553 in contig AL123456_GR.
KEGG	mtc:MT1604. mtu:Rv1553.
PATRIC	18125296. VBIMycTub22151_1762.
TIGR	MT1604.
Organism-specific databases
TubercuList	Rv1553.
Phylogenomic databases
GeneTree	EBGT00050000016375.
HOGENOM	HBG616382.
OMA	VGACSEV.
PhylomeDB	Q10761.
ProtClustDB	CLSK791244.
Family and domain databases
InterPro	IPR001450. 4Fe4S-bd_dom. IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR012675. Beta-grasp_ferredoxin-type. IPR001041. Ferredoxin. IPR012285. Fum_reductase_C. IPR009051. Helical_ferredxn. IPR004489. Succ_DH/fum_Rdtase_Fe-S. [Graphical view]
Gene3D	G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit. G3DSA:1.10.1060.10. Fum_reductase_C. 1 hit.
KO	K00245.
Pfam	PF00037. Fer4. 1 hit. [Graphical view]
SUPFAM	SSF54292. Ferredoxin. 1 hit. SSF46548. Helical_ferredxn. 1 hit.
TIGRFAMs	TIGR00384. DhsB. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. False negative. PS51085. 2FE2S_FER_2. False negative. PS00198. 4FE4S_FER_1. 1 hit. PS51379. 4FE4S_FER_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FRDB_MYCTU

Accession

Primary (citable) accession number: Q10761

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents