Putative formate dehydrogenase MW2229 - Staphylococcus aureus (strain MW2)

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Q7A057 (FDHL_STAAW) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 61. 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:
Putative formate dehydrogenase MW2229
EC=1.2.1.2

Gene names

Ordered Locus Names:

MW2229

Organism

Staphylococcus aureus (strain MW2) [Complete proteome] [HAMAP]

Taxonomic identifier

196620 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	984 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity

Formate + NAD⁺ = CO₂ + NADH.

Cofactor

Binds 1 2Fe-2S cluster By similarity.

Binds 4 4Fe-4S clusters By similarity.

Molybdenum (molybdopterin) By similarity.

Sequence similarities

In the C-terminal section; belongs to the prokaryotic molybdopterin-containing oxidoreductase family.

Contains 1 2Fe-2S ferredoxin-type domain.

Contains 2 4Fe-4S ferredoxin-type domains.

Ontologies

Keywords
Domain	Repeat
Ligand	2Fe-2S 4Fe-4S Iron Iron-sulfur Metal-binding Molybdenum NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	formate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	formate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular function	2 iron, 2 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 formate dehydrogenase (NAD+) activity Inferred from electronic annotation. Source: EC molybdenum ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on other nitrogenous compounds as donors Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 984

984

Putative formate dehydrogenase MW2229

PRO_0000304133

Regions

Domain

3 – 79

2Fe-2S ferredoxin-type

Domain

138 – 165

4Fe-4S ferredoxin-type 1

Domain

181 – 211

4Fe-4S ferredoxin-type 2

Region

252 – 984

733

Formate dehydrogenase

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

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

Metal binding

Iron-sulfur 2 (4Fe-4S); via tele nitrogen By similarity

Metal binding

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

Metal binding

102

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

Metal binding

109

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

Metal binding

147

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

Metal binding

150

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

Metal binding

153

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

Metal binding

157

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

Metal binding

190

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

Metal binding

193

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

Metal binding

196

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

Metal binding

200

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

Metal binding

264

Iron-sulfur 5 (4Fe-4S) By similarity

Metal binding

267

Iron-sulfur 5 (4Fe-4S) By similarity

Metal binding

271

Iron-sulfur 5 (4Fe-4S) By similarity

Metal binding

299

Iron-sulfur 5 (4Fe-4S) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q7A057 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 79140674B6A0C1D3
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FASTA

984

111,295

        10         20         30         40         50         60 
MQEHLVVTLD GKDYLVEPGT NLLEFIKSQD TFVPSICYNE SMGPIQTCDT CTVEIDGKIE 

        70         80         90        100        110        120 
RSCSTVIDRP MTVNTVNNDV KDAQKEALDR ILEKHMLYCT VCDYNNGDCE IHNTMDAWGL 

       130        140        150        160        170        180 
QHQTYEYKEK PYEKDYGPFY RYDPNQCILC GRCVEACQDI EVNETIRIDW DREHPRVIWD 

       190        200        210        220        230        240 
NDVPINESSC VSCGQCATVC PCNAMMEVNM EGNAGYMTDT EPGSLAAMID LTKKAEPGYG 

       250        260        270        280        290        300 
PLFAISDSEA EMRKERIKKT KTVCTYCGVG CSFEVWTKDR EILKVQPSHD SPANKIATCV 

       310        320        330        340        350        360 
KGKFSWGHIN SDQRLTKPLV RKNGEFHEVE WDEALNVIAD NFTSIKEKYG PDALSFISSS 

       370        380        390        400        410        420 
KATNEESYLM QKLARQVIGT NNVDNCSRYC QAPATKGLFR TVGHGGDSGS IEDLEKAAMS 

       430        440        450        460        470        480 
VLIGTNTAEA HPVIASRMKR AQKLFGQKIH VFDIRKHEMA ERADRFYQPK PGTDLAWLSA 

       490        500        510        520        530        540 
VTKYIIDHDL HDKAFIDEWV DDFDEYYKSL ETFTMAFAEE ATGIPESELI KFAEECAKAE 

       550        560        570        580        590        600 
SVVICWAMGI TQQDIGSDSS TAISNLLLVT GNYRRPGTGA YPLRGHNNVQ GCSDMGSMPD 

       610        620        630        640        650        660 
KITGYQSIEA DDIRAKFEKE YGVKLNPKAG KDNHEMVEGI HDGEVHSLYL YGEDTGIVDS 

       670        680        690        700        710        720 
NINFVQAAFE KLDFMVVQDE FLTFTATYAD VVLPASPSLE KDGTFTNTER RIQRLYQALE 

       730        740        750        760        770        780 
PLGDSKPDWK IFQAIANRLG FDWNYKHPSE IMDEVARLTP LYAGVSYDRL EGFNSLQWPV 

       790        800        810        820        830        840 
QPDGTDEPIL YLEGFNFDNG KAKLFPLSFD NYFKQDEIYD IHVNNGRLLE HFHEGNMTYQ 

       850        860        870        880        890        900 
TPMIKYKVPR AFVEISPELA EDRGIHEGAE VKLISETGEA VLQVHVTDRV KGKEIYIPLN 

       910        920        930        940        950        960 
NDAMENGDLG AINLLTNSDV DQYTDTPSYK RTSCRLEVIT KRGKSPLNPN NFRVNKKRHP 

       970        980 
QYSVQVQKKW ERSDYVFPGN QVDK

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References

[1]	"Genome and virulence determinants of high virulence community-acquired MRSA." Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K. Lancet 359:1819-1827(2002) [PubMed: 12044378] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MW2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000033 Genomic DNA. Translation: BAB96094.1.
RefSeq	NP_647046.1. NC_003923.1.
3D structure databases
HSSP	HSSP built from PDB template 1DUR based on UniProtKB P00193.
ProteinModelPortal	Q7A057.
ModBase	Search...
Protein-protein interaction databases
STRING	Q7A057.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTAT00000026025; EBSTAP00000025064; EBSTAG00000026024.
GeneID	1004347.
GenomeReviews	Gene locus MW2229 in contig BA000033_GR.
KEGG	sam:MW2229.
PATRIC	19571186. VBIStaAur44266_2303.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG3383.
GeneTree	EBGT00050000024767.
HOGENOM	HBG715033.
OMA	SARYCQA.
PhylomeDB	Q7A057.
ProtClustDB	CLSK865103.
Enzyme and pathway databases
BioCyc	SAUR196620:MW2229-MONOMER.
Family and domain databases
InterPro	IPR001450. 4Fe4S-bd_dom. IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR009010. Asp_de-COase-like_fold. IPR012675. Beta-grasp_ferredoxin-type. IPR001041. Ferredoxin. IPR006478. Formate_DH_asu. IPR012285. Fum_reductase_C. IPR006657. MoPterin_dinucl-bd_dom. IPR006656. Mopterin_OxRdtase. IPR006963. Mopterin_OxRdtase_Fe4S4_dom. IPR006655. Mopterin_OxRdtase_prok_CS. IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd. [Graphical view]
Gene3D	G3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit. G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit. G3DSA:1.10.1060.10. Fum_reductase_C. 1 hit.
KO	K00123.
Pfam	PF12838. Fer4_7. 1 hit. PF04879. Molybdop_Fe4S4. 1 hit. PF00384. Molybdopterin. 1 hit. PF01568. Molydop_binding. 1 hit. PF10588. NADH-G_4Fe-4S_3. 1 hit. [Graphical view]
PIRSF	PIRSF036643. FDH_alpha. 1 hit.
SMART	SM00926. Molybdop_Fe4S4. 1 hit. SM00929. NADH-G_4Fe-4S_3. 1 hit. [Graphical view]
SUPFAM	SSF50692. Asp_decarb_fold. 1 hit. SSF54292. Ferredoxin. 1 hit.
TIGRFAMs	TIGR01591. Fdh-alpha. 1 hit.
PROSITE	PS51085. 2FE2S_FER_2. 1 hit. PS00198. 4FE4S_FER_1. 1 hit. PS51379. 4FE4S_FER_2. 2 hits. PS00551. MOLYBDOPTERIN_PROK_1. 1 hit. PS00490. MOLYBDOPTERIN_PROK_2. False negative. PS00932. MOLYBDOPTERIN_PROK_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FDHL_STAAW

Accession

Primary (citable) accession number: Q7A057

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 61 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

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents