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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.Curated

Cofactori

Protein has several cofactor binding sites:

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

Subcellular locationi

GO - Cellular componenti

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

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

« Hide

        10         20         30         40         50
MLIKRRAFLK LTAAGATLSA FGGLGVDLAP AKAQAATMAL KTVDAKQTTS
60 70 80 90 100
VCCYCSVGCG LIVHTDKKTN RAINVEGDPD HPINEGSLCA KGASTWQLAE
110 120 130 140 150
NERRPANPLY RAPGSDQWEE KSWDWMLDTI AERVAKTREA TFVTKNAKGQ
160 170 180 190 200
VVNRCDGIAS VGSAAMDNEE CWIYQAWLRS LGLFYIEHQA RIUHSATVAA
210 220 230 240 250
LAESYGRGAM TNHWIDLKNS DVILMMGSNP AENHPISFKW VMRAKDKGAT
260 270 280 290 300
LIHVDPRYTR TSTKCDLYAP LRSGSDIAFL NGMTKYILEK ELYFKDYVVN
310 320 330 340 350
YTNASFIVGE GFAFEEGLFA GYNKETRKYD KSKWGFERDE NGNPKRDETL
360 370 380 390 400
KHPRCVFQIM KKHYERYDLD KISAICGTPK ELILKVYDAY CATGKPDKAG
410 420 430 440 450
TIMYAMGWTQ HTVGVQNIRA MSINQLLLGN IGVAGGGVNA LRGEANVQGS
460 470 480 490 500
TDHGLLMHIY PGYLGTARAS IPTYEEYTKK FTPVSKDPQS ANWWSNFPKY
510 520 530 540 550
SASYIKSMWP DADLNEAYGY LPKGEDGKDY SWLTLFDDMF QGKIKGFFAW
560 570 580 590 600
GQNPACSGAN SNKTREALTK LDWMVNVNIF DNETGSFWRG PDMDPKKIKT
610 620 630 640 650
EVFFLPCAVA IEKEGSISNS GRWMQWRYVG PEPRKNAIPD GDLIVELAKR
660 670 680 690 700
VQKLLAKTPG KLAAPVTKLK TDYWVNDHGH FDPHKIAKLI NGFALKDFKV
710 720 730 740 750
GDVEYKAGQQ IATFGHLQAD GSTTSGCWIY TGSYTEKGNM AARRDKTQTD
760 770 780 790 800
MQAKIGLYPG WTWAWPVNRR IIYNRASVDL NGKPYAPEKA VVEWNAAEKK
810 820 830 840 850
WVGDVPDGPW PPQADKEKGK RAFIMKPEGY AYLYGPGRED GPLPEYYEPM
860 870 880 890 900
ECPVIEHPFS KTLHNPTALH FATEEKAVCD PRYPFICSTY RVTEHWQTGL
910 920 930 940 950
MTRNTPWLLE AEPQMFCEMS EELATLRGIK NGDKVILESV RGKLWAKAII
960 970 980 990 1000
TKRIKPFAIQ GQQVHMVGIP WHYGWSFPKN GGDAANILTP SVGDPNTGIP
1010
ETKAFMVNVT KA
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:
EMBLi
GenBanki
DDBJi
Links Updated
AJ318781 Genomic DNA. Translation: CAC86667.1.

Keywords - Coding sequence diversityi

Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ318781 Genomic DNA. Translation: CAC86667.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 77 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