Putative formate dehydrogenase SAR2393 - Staphylococcus aureus (strain MRSA252)

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Names and origin

Protein names

Recommended name:
Putative formate dehydrogenase SAR2393
EC=1.2.1.2

Gene names

Ordered Locus Names:

SAR2393

Organism

Staphylococcus aureus (strain MRSA252) [Complete proteome] [HAMAP]

Taxonomic identifier

282458 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

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Protein attributes

Sequence length	984 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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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.

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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 oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
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 activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW molybdenum ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 984

984

Putative formate dehydrogenase SAR2393

PRO_0000304130

Regions

Domain

3 – 79

77

2Fe-2S ferredoxin-type

Domain

138 – 165

28

4Fe-4S ferredoxin-type 1

Domain

181 – 211

31

4Fe-4S ferredoxin-type 2

Region

252 – 984

733

Formate dehydrogenase

Sites

Metal binding

37

1

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

Metal binding

48

1

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

Metal binding

51

1

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

Metal binding

63

1

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

Metal binding

95

1

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

Metal binding

99

1

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

Metal binding

102

1

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

Metal binding

109

1

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

Metal binding

147

1

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

Metal binding

150

1

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

Metal binding

153

1

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

Metal binding

157

1

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

Metal binding

190

1

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

Metal binding

193

1

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

Metal binding

196

1

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

Metal binding

200

1

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

Metal binding

264

1

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

Metal binding

267

1

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

Metal binding

271

1

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

Metal binding

299

1

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

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Sequences

Sequence

Length

Mass (Da)

Tools

Q6GEC4-1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: FE1153208DAD5F33
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FASTA

984

111,342

        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 ELNETIRIDW 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 NFTSIKEKHG 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 HDKAFIEEWV EDFDEYYKSL ETFTMAFAEE ATGIPEAELI KFAEECAKAE 

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

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

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

       730        740        750        760        770        780 
PLGDSKPDWK IFQAIANKLS FDWNYKHPSE IMDEIARLTP LYAGVSYERL EGFNSLQWPV 

       790        800        810        820        830        840 
HPDGTDEPIL YLEGFNFDNG KAKLFPLSFD NYFKQDEVYD IHVNNGRLLE HFHEGNMTYQ 

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

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

       970        980 
QYSVQVQKKW ERPDYVFPGN QVDK

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References

[1]

"Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance."
Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C.

Parkhill J.
Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed: 15213324] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases
	BX571856 Genomic DNA. Translation: CAG41375.1.
RefSeq	YP_041749.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6GEC4.
Genome annotation databases
GeneID	2859010.
GenomeReviews	Gene locus SAR2393 in contig BX571856_GR.
KEGG	sar:SAR2393.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6GEC4.
OMA	NETISID.
Enzyme and pathway databases
BioCyc	SAUR282458:SAR2393-MON.
Family and domain databases
InterPro	IPR017896. 4Fe4S_Fe-S-bd. IPR001450. 4Fe4S_Fe_S_bd_subgr. IPR017900. 4Fe4S_Fe_S_CS. IPR009010. Asp_de-COase-like_fold. IPR001041. Ferredoxin. IPR006478. Formate_DH_asu. IPR006656. Mopterin_OxRdtase. IPR006963. Mopterin_OxRdtase_Fe4S4. IPR006655. Mopterin_OxRdtase_prok_CS. IPR006657. MPT_dinuc_bd. IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd. [Graphical view]
Gene3D	G3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit.
Pfam	PF00111. Fer2. 1 hit. PF00037. Fer4. 2 hits. PF04879. Molybdop_Fe4S4. 1 hit. PF00384. Molybdopterin. 1 hit. PF01568. Molydop_binding. 1 hit. PF10588. NADH-G_4Fe-4S_3. 1 hit. [Graphical view]
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...

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Entry information

Entry name

FDHL_STAAR

Accession

Primary (citable) accession number: Q6GEC4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	July 19, 2004
Last modified:	November 3, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

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

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents