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Protein

Formate dehydrogenase subunit alpha

Gene

fdhA

Organism
Desulfovibrio gigas
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi52Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation1 Publication1
Metal bindingi55Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation1 Publication1
Metal bindingi59Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation1 Publication1
Metal bindingi89Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation1 Publication1
Metal bindingi193Tungsten1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi394 – 3981 Publication5

GO - Molecular functioni

GO - Biological processi

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

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

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 35Tat-type signalAdd BLAST35
ChainiPRO_000001914936 – 1012Formate dehydrogenase subunit alphaAdd BLAST977

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

11012
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni41 – 44Combined sources4
Beta strandi45 – 51Combined sources7
Beta strandi53 – 55Combined sources3
Beta strandi60 – 65Combined sources6
Turni67 – 69Combined sources3
Beta strandi72 – 77Combined sources6
Turni82 – 86Combined sources5
Helixi90 – 93Combined sources4
Helixi95 – 99Combined sources5
Beta strandi109 – 111Combined sources3
Helixi123 – 141Combined sources19
Beta strandi142 – 145Combined sources4
Beta strandi151 – 155Combined sources5
Beta strandi157 – 161Combined sources5
Helixi168 – 180Combined sources13
Helixi190 – 193Combined sources4
Helixi195 – 205Combined sources11
Helixi215 – 219Combined sources5
Beta strandi221 – 227Combined sources7
Helixi230 – 233Combined sources4
Helixi237 – 246Combined sources10
Beta strandi250 – 254Combined sources5
Helixi262 – 264Combined sources3
Beta strandi266 – 269Combined sources4
Helixi276 – 289Combined sources14
Helixi295 – 301Combined sources7
Helixi303 – 305Combined sources3
Beta strandi306 – 308Combined sources3
Turni324 – 327Combined sources4
Helixi331 – 334Combined sources4
Helixi356 – 364Combined sources9
Helixi369 – 376Combined sources8
Helixi380 – 391Combined sources12
Helixi392 – 394Combined sources3
Beta strandi400 – 404Combined sources5
Helixi411 – 427Combined sources17
Beta strandi431 – 433Combined sources3
Beta strandi437 – 440Combined sources4
Helixi447 – 452Combined sources6
Turni461 – 463Combined sources3
Helixi474 – 481Combined sources8
Helixi493 – 496Combined sources4
Helixi497 – 508Combined sources12
Helixi514 – 520Combined sources7
Helixi532 – 540Combined sources9
Beta strandi546 – 551Combined sources6
Helixi554 – 557Combined sources4
Beta strandi558 – 560Combined sources3
Helixi561 – 568Combined sources8
Beta strandi572 – 580Combined sources9
Turni583 – 586Combined sources4
Helixi587 – 589Combined sources3
Helixi595 – 597Combined sources3
Beta strandi601 – 607Combined sources7
Helixi610 – 612Combined sources3
Beta strandi615 – 618Combined sources4
Beta strandi623 – 627Combined sources5
Helixi640 – 657Combined sources18
Helixi664 – 668Combined sources5
Helixi671 – 674Combined sources4
Helixi683 – 691Combined sources9
Beta strandi693 – 696Combined sources4
Beta strandi698 – 700Combined sources3
Beta strandi703 – 705Combined sources3
Helixi714 – 716Combined sources3
Helixi728 – 730Combined sources3
Beta strandi733 – 735Combined sources3
Helixi740 – 742Combined sources3
Helixi750 – 755Combined sources6
Beta strandi761 – 764Combined sources4
Turni765 – 768Combined sources4
Helixi774 – 777Combined sources4
Helixi787 – 789Combined sources3
Beta strandi791 – 795Combined sources5
Turni796 – 799Combined sources4
Beta strandi800 – 804Combined sources5
Turni816 – 818Combined sources3
Beta strandi826 – 829Combined sources4
Beta strandi851 – 853Combined sources3
Beta strandi885 – 890Combined sources6
Helixi900 – 903Combined sources4
Helixi906 – 911Combined sources6
Beta strandi916 – 919Combined sources4
Helixi921 – 927Combined sources7
Beta strandi934 – 939Combined sources6
Beta strandi942 – 950Combined sources9
Beta strandi957 – 959Combined sources3
Beta strandi962 – 964Combined sources3
Beta strandi966 – 971Combined sources6
Helixi985 – 987Combined sources3
Beta strandi991 – 994Combined sources4
Beta strandi996 – 1000Combined sources5
Beta strandi1005 – 1011Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H0HX-ray1.80A/K36-1012[»]
ProteinModelPortaliQ934F5.
SMRiQ934F5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ934F5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini45 – 1034Fe-4S Mo/W bis-MGD-typePROSITE-ProRule annotationAdd BLAST59

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-alph_fdnG.
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)DescriptionActionsGraphical viewLength
Non-standard residuei193Selenocysteine1 Publication1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H0HX-ray1.80A/K36-1012[»]
ProteinModelPortaliQ934F5.
SMRiQ934F5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ934F5.

Family and domain databases

InterProiIPR009010. Asp_de-COase-like_dom.
IPR006443. Formate-DH-alph_fdnG.
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]
ProtoNetiSearch...

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 2, 2016
This is version 82 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.