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Q934F5

- FDHA_DESGI

UniProt

Q934F5 - FDHA_DESGI

Protein

Formate dehydrogenase subunit alpha

Gene

fdhA

Organism
Desulfovibrio gigas
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 2 (26 Feb 2008)
      Previous versions | rss
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    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.Curated

    Cofactori

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

    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 PublicationPROSITE-ProRule annotation
    Metal bindingi55 – 551Iron-sulfur (4Fe-4S)1 PublicationPROSITE-ProRule annotation
    Metal bindingi59 – 591Iron-sulfur (4Fe-4S)1 PublicationPROSITE-ProRule annotation
    Metal bindingi89 – 891Iron-sulfur (4Fe-4S)1 PublicationPROSITE-ProRule annotation
    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

    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:fdhA1 Publication
    OrganismiDesulfovibrio gigasImported
    Taxonomic identifieri879 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3535Tat-type signalAdd
    BLAST
    Chaini36 – 1012977Formate dehydrogenase subunit alphaPRO_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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ934F5.

    Family & Domainsi

    Domains and Repeats

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

    Sequence similaritiesi

    Contains 1 4Fe-4S Mo/W bis-MGD-type domain.PROSITE-ProRule annotation

    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 – 1931Selenocysteine1 Publication

    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: October 1, 2014
    This is version 75 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