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Q934F5

- FDHA_DESGI

UniProt

Q934F5 - FDHA_DESGI

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Protein

Formate dehydrogenase subunit alpha

Gene
fdhA
Organism
Desulfovibrio gigas
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Alpha chain of the formate dehydrogenase (FDH) catalyze the reversible two-electron oxidation of formate to carbon dioxide. FDH loses activity in the presence of air, but this activity can be restored. The alpha subunit of formate dehydrogenase forms the active site.

Catalytic activityi

Formate + NAD+ = CO2 + NADH.

Cofactori

Binds 1 4Fe-4S cluster per subunit.2 Publications
Binds 1 tungsten-bis(molybdopterin guanine dinucleotide) (W-bis-MGD) cofactor per subunit.2 Publications

pH dependencei

Optimum pH is 7.5-8.0.

Temperature dependencei

Optimum temperature is 56 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi52 – 521Iron-sulfur (4Fe-4S)1 Publication
Metal bindingi55 – 551Iron-sulfur (4Fe-4S)1 Publication
Metal bindingi59 – 591Iron-sulfur (4Fe-4S)1 Publication
Metal bindingi89 – 891Iron-sulfur (4Fe-4S)1 Publication
Metal bindingi193 – 1931Tungsten1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi394 – 39851 Publication

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. electron carrier activity Source: InterPro
  3. formate dehydrogenase (NAD+) activity Source: UniProtKB-EC
  4. molybdenum ion binding Source: InterPro

GO - Biological processi

  1. cellular respiration Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

4Fe-4S, Calcium, Iron, Iron-sulfur, Metal-binding, NAD, Tungsten

Enzyme and pathway databases

BRENDAi1.2.2.1. 1907.

Names & Taxonomyi

Protein namesi
Recommended name:
Formate dehydrogenase subunit alpha (EC:1.2.1.2)
Short name:
FDH subunit alpha
Alternative name(s):
Formate dehydrogenase large subunit
Gene namesi
Name:fdhA
OrganismiDesulfovibrio gigas
Taxonomic identifieri879 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
  2. periplasmic space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535Tat-type signal1 PublicationAdd
BLAST
Chaini36 – 1012977Formate dehydrogenase subunit alpha1 PublicationPRO_0000019149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi852 ↔ 8791 Publication

Post-translational modificationi

The disulfide bond is likely to be broken in the active form of this enzyme.1 Publication
Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Heterodimer of alpha (FdhA) and beta (FdhB) subunits.3 Publications

Structurei

Secondary structure

1
1012
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni41 – 444
Beta strandi45 – 517
Beta strandi53 – 553
Beta strandi60 – 656
Turni67 – 693
Beta strandi72 – 776
Turni82 – 865
Helixi90 – 934
Helixi95 – 995
Beta strandi109 – 1113
Helixi123 – 14119
Beta strandi142 – 1454
Beta strandi151 – 1555
Beta strandi157 – 1615
Helixi168 – 18013
Helixi190 – 1934
Helixi195 – 20511
Helixi215 – 2195
Beta strandi221 – 2277
Helixi230 – 2334
Helixi237 – 24610
Beta strandi250 – 2545
Helixi262 – 2643
Beta strandi266 – 2694
Helixi276 – 28914
Helixi295 – 3017
Helixi303 – 3053
Beta strandi306 – 3083
Turni324 – 3274
Helixi331 – 3344
Helixi356 – 3649
Helixi369 – 3768
Helixi380 – 39112
Helixi392 – 3943
Beta strandi400 – 4045
Helixi411 – 42717
Beta strandi431 – 4333
Beta strandi437 – 4404
Helixi447 – 4526
Turni461 – 4633
Helixi474 – 4818
Helixi493 – 4964
Helixi497 – 50812
Helixi514 – 5207
Helixi532 – 5409
Beta strandi546 – 5516
Helixi554 – 5574
Beta strandi558 – 5603
Helixi561 – 5688
Beta strandi572 – 5809
Turni583 – 5864
Helixi587 – 5893
Helixi595 – 5973
Beta strandi601 – 6077
Helixi610 – 6123
Beta strandi615 – 6184
Beta strandi623 – 6275
Helixi640 – 65718
Helixi664 – 6685
Helixi671 – 6744
Helixi683 – 6919
Beta strandi693 – 6964
Beta strandi698 – 7003
Beta strandi703 – 7053
Helixi714 – 7163
Helixi728 – 7303
Beta strandi733 – 7353
Helixi740 – 7423
Helixi750 – 7556
Beta strandi761 – 7644
Turni765 – 7684
Helixi774 – 7774
Helixi787 – 7893
Beta strandi791 – 7955
Turni796 – 7994
Beta strandi800 – 8045
Turni816 – 8183
Beta strandi826 – 8294
Beta strandi851 – 8533
Beta strandi885 – 8906
Helixi900 – 9034
Helixi906 – 9116
Beta strandi916 – 9194
Helixi921 – 9277
Beta strandi934 – 9396
Beta strandi942 – 9509
Beta strandi957 – 9593
Beta strandi962 – 9643
Beta strandi966 – 9716
Helixi985 – 9873
Beta strandi991 – 9944
Beta strandi996 – 10005
Beta strandi1005 – 10117

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H0HX-ray1.80A/K36-1012[»]
ProteinModelPortaliQ934F5.

Miscellaneous databases

EvolutionaryTraceiQ934F5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 103594Fe-4S Mo/W bis-MGD-typeAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR009010. Asp_de-COase-like_dom.
IPR006443. Formate_DH_asu_anaerob.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR006655. Mopterin_OxRdtase_prok_CS.
IPR027467. MopterinOxRdtase_cofactor_BS.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SMARTiSM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
TIGRFAMsiTIGR01553. formate-DH-alph. 1 hit.
PROSITEiPS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q934F5-1 [UniParc]FASTAAdd to Basket

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MLIKRRAFLK LTAAGATLSA FGGLGVDLAP AKAQAATMAL KTVDAKQTTS     50
VCCYCSVGCG LIVHTDKKTN RAINVEGDPD HPINEGSLCA KGASTWQLAE 100
NERRPANPLY RAPGSDQWEE KSWDWMLDTI AERVAKTREA TFVTKNAKGQ 150
VVNRCDGIAS VGSAAMDNEE CWIYQAWLRS LGLFYIEHQA RIUHSATVAA 200
LAESYGRGAM TNHWIDLKNS DVILMMGSNP AENHPISFKW VMRAKDKGAT 250
LIHVDPRYTR TSTKCDLYAP LRSGSDIAFL NGMTKYILEK ELYFKDYVVN 300
YTNASFIVGE GFAFEEGLFA GYNKETRKYD KSKWGFERDE NGNPKRDETL 350
KHPRCVFQIM KKHYERYDLD KISAICGTPK ELILKVYDAY CATGKPDKAG 400
TIMYAMGWTQ HTVGVQNIRA MSINQLLLGN IGVAGGGVNA LRGEANVQGS 450
TDHGLLMHIY PGYLGTARAS IPTYEEYTKK FTPVSKDPQS ANWWSNFPKY 500
SASYIKSMWP DADLNEAYGY LPKGEDGKDY SWLTLFDDMF QGKIKGFFAW 550
GQNPACSGAN SNKTREALTK LDWMVNVNIF DNETGSFWRG PDMDPKKIKT 600
EVFFLPCAVA IEKEGSISNS GRWMQWRYVG PEPRKNAIPD GDLIVELAKR 650
VQKLLAKTPG KLAAPVTKLK TDYWVNDHGH FDPHKIAKLI NGFALKDFKV 700
GDVEYKAGQQ IATFGHLQAD GSTTSGCWIY TGSYTEKGNM AARRDKTQTD 750
MQAKIGLYPG WTWAWPVNRR IIYNRASVDL NGKPYAPEKA VVEWNAAEKK 800
WVGDVPDGPW PPQADKEKGK RAFIMKPEGY AYLYGPGRED GPLPEYYEPM 850
ECPVIEHPFS KTLHNPTALH FATEEKAVCD PRYPFICSTY RVTEHWQTGL 900
MTRNTPWLLE AEPQMFCEMS EELATLRGIK NGDKVILESV RGKLWAKAII 950
TKRIKPFAIQ GQQVHMVGIP WHYGWSFPKN GGDAANILTP SVGDPNTGIP 1000
ETKAFMVNVT KA 1012
Length:1,012
Mass (Da):113,271
Last modified:February 26, 2008 - v2
Checksum:i23CDC4594334D51F
GO

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei193 – 1931Selenocysteine

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ318781 Genomic DNA. Translation: CAC86667.1.

Keywords - Coding sequence diversityi

Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ318781 Genomic DNA. Translation: CAC86667.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1H0H X-ray 1.80 A/K 36-1012 [» ]
ProteinModelPortali Q934F5.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 1.2.2.1. 1907.

Miscellaneous databases

EvolutionaryTracei Q934F5.

Family and domain databases

InterProi IPR009010. Asp_de-COase-like_dom.
IPR006443. Formate_DH_asu_anaerob.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR006655. Mopterin_OxRdtase_prok_CS.
IPR027467. MopterinOxRdtase_cofactor_BS.
IPR006311. TAT_signal.
[Graphical view ]
Pfami PF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view ]
SMARTi SM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view ]
SUPFAMi SSF50692. SSF50692. 1 hit.
TIGRFAMsi TIGR01553. formate-DH-alph. 1 hit.
PROSITEi PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS00932. MOLYBDOPTERIN_PROK_3. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Gene sequence and the 1.8 A crystal structure of the tungsten-containing formate dehydrogenase from Desulfovibrio gigas."
    Raaijmakers H., Macieira S.I.M.G., Dias J.M., Teixeira S., Bursakov S., Huber R., Moura J.J.G., Moura I., Romao M.J.
    Structure 10:1261-1272(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, COFACTOR, DISULFIDE BOND, CALCIUM-BINDING, METAL-BINDING, X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH FDHB.
    Strain: ATCC 19364 / DSM 1382 / NCIB 9332 / VKM B-1759.
  2. "Properties of formate dehydrogenase from Desulfivibrio gigas."
    Riederer-Henderson M.A., Peck H.D. Jr.
    Can. J. Microbiol. 32:430-435(1986)
    Cited for: CHARACTERIZATION.
  3. "Purification and characterization of a tungsten-containing formate dehydrogenase from Desulfovibrio gigas."
    Almendra M.J., Brondino C.D., Gavel O., Pereira A.S., Tavares P., Bursakov S., Duarte R., Caldeira J., Moura J.J.G., Moura I.
    Biochemistry 38:16366-16372(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, SUBUNIT.
    Strain: ATCC 19364 / DSM 1382 / NCIB 9332 / VKM B-1759.
  4. "Tungsten-containing formate dehydrogenase from Desulfovibrio gigas: metal identification and preliminary structural data by multi-wavelength crystallography."
    Raaijmakers H., Teixeira S., Dias J.M., Almendra M.J., Brondino C.D., Moura I., Moura J.J.G., Romao M.J.
    J. Biol. Inorg. Chem. 6:398-404(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR, SUBUNIT.

Entry informationi

Entry nameiFDHA_DESGI
AccessioniPrimary (citable) accession number: Q934F5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: February 26, 2008
Last modified: February 19, 2014
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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