Putative formate dehydrogenase SAB2186c - Staphylococcus aureus (strain bovine RF122 / ET3-1)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Putative formate dehydrogenase SAB2186c
EC=1.2.1.2

Gene names

Ordered Locus Names:

SAB2186c

Organism

Staphylococcus aureus (strain bovine RF122 / ET3-1) [Complete proteome] [HAMAP]

Taxonomic identifier

273036 [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 SAB2186c

PRO_0000304128

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

Sequences

Sequence

Length

Mass (Da)

Tools

Q2YYT1 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: D9148E8BB9B4DA02
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FASTA

984

111,309

        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 EPGSLAAMVD 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 HDKAFIEEWV EDFDEYYKSL ETFTMAFAEE ATGIPEAELI KFAEECAKAE 

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

       610        620        630        640        650        660 
KITGYQSIEA DDIRAKFEKE YGVKLNPKVG KDNHEMVEGV HDGEIHSLYL YGEDTGIVDS 

       670        680        690        700        710        720 
NINFVQAAFE NLDFMVVQDE FLTFTATFAD VVLPASPSLE KDGTFTNTER RIQRLYQALK 

       730        740        750        760        770        780 
PLGESKPDWK IFQAIANKLG FDWNYKHPSE IMDEIARLTP LYAGVSYERL EGFNSLQWPV 

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

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

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

       970        980 
QYSVQVQKKW ERPDYVFPGN QVDK

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References

[1]	"Molecular correlates of host specialization in Staphylococcus aureus." Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V. PLoS ONE 2:E1120-E1120(2007) [PubMed: 17971880] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: bovine RF122 / ET3-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ938182 Genomic DNA. Translation: CAI81875.1.
RefSeq	YP_417643.1. NC_007622.1.
3D structure databases
HSSP	HSSP built from PDB template 2IV2 based on UniProtKB P07658.
ProteinModelPortal	Q2YYT1.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2YYT1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTAT00000013522; EBSTAP00000013179; EBSTAG00000013521.
GeneID	3793615.
GenomeReviews	Gene locus SAB2186c in contig AJ938182_GR.
KEGG	sab:SAB2186c.
NMPDR	fig\|273036.3.peg.2124.
PATRIC	19525415. VBIStaAur92441_2303.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG3383.
GeneTree	EBGT00050000024767.
HOGENOM	HBG715033.
OMA	SARYCQA.
PhylomeDB	Q2YYT1.
ProtClustDB	CLSK865103.
Enzyme and pathway databases
BioCyc	SAUR273036:SAB2186C-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_STAAB

Accession

Primary (citable) accession number: Q2YYT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	December 20, 2005
Last modified:	January 25, 2012
This is version 53 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

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