Formate dehydrogenase major subunit precursor - Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Formate dehydrogenase major subunit
EC=1.2.1.2

Alternative name(s):
Formate dehydrogenase subunit alpha
Short name=FDH subunit alpha

Gene names

Name:	fdxG
Ordered Locus Names:	HI_0006

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	1028 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Allows to use formate as major electron donor during anaerobic respiration. Subunit alpha possibly forms the active site.
Catalytic activity	Formate + NAD⁺ = CO₂ + NADH.
Cofactor	Molybdenum (molybdopterin). Binds 1 4Fe-4S cluster Potential.
Subunit structure	Formate dehydrogenase is a membrane-bound complex, formed by subunits alpha, beta and gamma.
Subcellular location	Periplasm Potential.
Post-translational modification	Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Sequence similarities	Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.

Ontologies

Keywords
Cellular component	Periplasm
Coding sequence diversity	Selenocysteine
Domain	Signal
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding Molybdenum NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular respiration Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	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

Signal peptide

1 – 33

33

Tat-type signal Potential

Chain

34 – 1028

995

Formate dehydrogenase major subunit

PRO_0000063224

Sites

Metal binding

50

1

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

Metal binding

53

1

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

Metal binding

57

1

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

Metal binding

100

1

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

Amino acid modifications

Non-standard residue

204

1

Selenocysteine Probable

Sequences

Sequence

Length

Mass (Da)

Tools

P46448 [UniParc].

Last modified February 26, 2008. Version 2.
Checksum: 4A2E55B78B301300
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FASTA

1,028

115,451

        10         20         30         40         50         60 
MQVSRRKFFK ICAGGMAGTS AAMLGFAPAN VLAAPREYKL LRAFESRNTC TYCAVSCGML 

        70         80         90        100        110        120 
LYSTGKPYNS LSSHTGTNTR SKLFHIEGDP DHPVSRGALC PKGAGSLDYV NSESRSLYPQ 

       130        140        150        160        170        180 
YRAPGSDKWE RISWKDAIKR IARLMKDDRD ANFVEKDSNG KTVNRWATTG IMTASAMSNE 

       190        200        210        220        230        240 
AALLTQKWIR MLGMVPVCNQ ANTUHGPTVA SLAPSFGRGA MTNNWVDIKN ANLIIVQGGN 

       250        260        270        280        290        300 
PAEAHPVGFR WAIEAKKNGA KIIVIDPRFN RTASVADLHA PIRSGSDITF LMGVIRYLLE 

       310        320        330        340        350        360 
TNQIQHEYVK HYTNASFLID EGFKFEDGLF VGYNEEKRNY DKSKWNYQFD ENGHAKRDMT 

       370        380        390        400        410        420 
LQHPRCVINI LKEHVSRYTP EMVERITGVK QKLFLQICEE IGKTSVPNKT MTHLYALGFT 

       430        440        450        460        470        480 
EHSIGTQNIR SMAIIQLLLG NMGMPGGGIN ALRGHSNVQG TTDMGLLPMS LPGYMRLPND 

       490        500        510        520        530        540 
KDTSYDQYIN AITPKDIVPN QVNYYRHTSK FFVSMMKTFY GDNATKENGW GFDFLPKADR 

       550        560        570        580        590        600 
LYDPITHVKL MNEGKLHGWI LQGFNVLNSL PNKNKTLSGM SKLKYLVVMD PLQTESSEFW 

       610        620        630        640        650        660 
RNFGESNNVN PAEIQTEVFR LPTTCFAEEE GSIVNSGRWT QWHWKGCDQP GEALPDVDIL 

       670        680        690        700        710        720 
SMLREEMHEL YKKEGGQGIE SFEAMTWNYA QPHSPSAVEL AKELNGYALE DLYDPNGNLM 

       730        740        750        760        770        780 
YKKGQLLNGF AHLRDDGTTT SGNWLYVGQW TEKGNQTANR DNSDPSGLGC TIGWGFAWPA 

       790        800        810        820        830        840 
NRRVLYSRAS LDINGNPWDK NRQLIKWNGK NWNWFDIADY GTQPPGSDTG PFIMSAEGVG 

       850        860        870        880        890        900 
RLFAVDKIAN GPMPEHYEPV ESPIDTNPFH PNVVTDPTLR IYKEDREFIG SNKEYPFVAT 

       910        920        930        940        950        960 
TYRLTEHFHS WTAQSALNII AQPQQFVEIG EKLAAEKGIQ KGDMVKITSR RGYIKAVAVV 

       970        980        990       1000       1010       1020 
TKRLKDLEID GRVVHHIGLP IHWNMKALNG KGNRGFSTNT LTPSWGEAIT QTPEYKTFLV 


NIEKVGEA

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References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd."
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I.

Venter J.C.
Science 269:496-512(1995) [PubMed: 7542800] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. No translation available.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GenomeReviews	Gene locus HI_0006 in contig L42023_GR.
TIGR	HI_0006.
Phylogenomic databases
HOGENOM	HBG436656.
OMA	GWVTEAM.
Family and domain databases
InterPro	IPR009010. Asp_de-COase-like_fold. IPR006443. Formate_DH_asu_anaerob. IPR006657. MoPterin_dinucl-bd_dom. IPR006656. Mopterin_OxRdtase. IPR006963. Mopterin_OxRdtase_Fe4S4_dom. IPR006655. Mopterin_OxRdtase_prok_CS. IPR006311. TAT_signal. [Graphical view]
Gene3D	G3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit.
Pfam	PF04879. Molybdop_Fe4S4. 1 hit. PF00384. Molybdopterin. 1 hit. PF01568. Molydop_binding. 1 hit. [Graphical view]
SMART	SM00926. Molybdop_Fe4S4. 1 hit. [Graphical view]
SUPFAM	SSF50692. Asp_decarb_fold. 1 hit.
TIGRFAMs	TIGR01553. Formate-DH-alph. 1 hit.
PROSITE	PS00551. MOLYBDOPTERIN_PROK_1. 1 hit. PS00490. MOLYBDOPTERIN_PROK_2. False negative. PS00932. MOLYBDOPTERIN_PROK_3. 1 hit. PS51318. TAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FDXG_HAEIN

Accession

Primary (citable) accession number: P46448

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	February 26, 2008
Last modified:	October 19, 2011
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names

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

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents