FDNGA_DESVH
ID FDNGA_DESVH Reviewed; 1012 AA.
AC Q727P3;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Formate dehydrogenase 2 subunit alpha (cytochrome c-553) {ECO:0000303|PubMed:16274230};
DE Short=FDH2 subunit alpha (cytochrome c-553) {ECO:0000303|PubMed:16274230};
DE EC=1.17.2.3 {ECO:0000269|PubMed:21498650, ECO:0000269|PubMed:8566699};
DE AltName: Full=Formate dehydrogenase large subunit (cytochrome c-553);
DE Flags: Precursor;
GN Name=fdnG-3 {ECO:0000312|EMBL:AAS97284.1};
GN OrderedLocusNames=DVU_2812 {ECO:0000312|EMBL:AAS97284.1};
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
RN [2]
RP PROTEIN SEQUENCE OF 34-38, SUBUNIT, INDUCTION BY MOLYBDENUM, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RX PubMed=21498650; DOI=10.1128/jb.00042-11;
RA da Silva S.M., Pimentel C., Valente F.M., Rodrigues-Pousada C.,
RA Pereira I.A.;
RT "Tungsten and molybdenum regulation of formate dehydrogenase expression in
RT Desulfovibrio vulgaris Hildenborough.";
RL J. Bacteriol. 193:2909-2916(2011).
RN [3]
RP PROTEIN SEQUENCE OF 35-47, SUBUNIT, SUBCELLULAR LOCATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8566699; DOI=10.1111/j.1574-6968.1995.tb07875.x;
RA Sebban C., Blanchard L., Bruschi M., Guerlesquin F.;
RT "Purification and characterization of the formate dehydrogenase from
RT Desulfovibrio vulgaris Hildenborough.";
RL FEMS Microbiol. Lett. 133:143-149(1995).
RN [4]
RP SUBUNIT, AND NOMENCLATURE.
RX PubMed=16274230; DOI=10.1021/bi0515366;
RA ElAntak L., Dolla A., Durand M.C., Bianco P., Guerlesquin F.;
RT "Role of the tetrahemic subunit in Desulfovibrio vulgaris hildenborough
RT formate dehydrogenase.";
RL Biochemistry 44:14828-14834(2005).
CC -!- FUNCTION: Alpha chain of the formate dehydrogenase (FDH) that catalyzes
CC the reversible two-electron oxidation of formate to carbon dioxide. The
CC alpha subunit of formate dehydrogenase forms the active site.
CC {ECO:0000269|PubMed:8566699}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome c553] + formate = CO2 + 2 Fe(II)-
CC [cytochrome c553] + H(+); Xref=Rhea:RHEA:15189, Rhea:RHEA-COMP:10433,
CC Rhea:RHEA-COMP:10434, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.17.2.3;
CC Evidence={ECO:0000269|PubMed:21498650, ECO:0000269|PubMed:8566699};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q934F5};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:Q934F5};
CC -!- COFACTOR:
CC Name=W-bis(molybdopterin guanine dinucleotide); Xref=ChEBI:CHEBI:60537;
CC Evidence={ECO:0000269|PubMed:21498650};
CC Note=Binds 1 W-bis(molybdopterin guanine dinucleotide) (W-bis-MGD)
CC cofactor per subunit. {ECO:0000269|PubMed:21498650};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.7 mM for formate (at pH 9.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:8566699};
CC KM=8 uM for formate (at pH 7.6) {ECO:0000269|PubMed:21498650};
CC Vmax=77 umol/min/mg enzyme (at pH 7.6) {ECO:0000269|PubMed:21498650};
CC Note=Measurements have been done with the heterotrimer complex. kcat
CC is 262 sec(-1) with formate as substrate (at pH 7.6).
CC {ECO:0000269|PubMed:21498650};
CC pH dependence:
CC Optimum pH is 9.5. {ECO:0000269|PubMed:8566699};
CC Temperature dependence:
CC Optimum temperature is 51 degrees Celsius.
CC {ECO:0000269|PubMed:8566699};
CC -!- SUBUNIT: Heterotrimer of cytochrome c3 FDH2C and formate dehydrogenase
CC FDH2 alpha and beta subunits that forms the FdhABC(3) complex.
CC {ECO:0000269|PubMed:16274230, ECO:0000269|PubMed:21498650,
CC ECO:0000269|PubMed:8566699}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:8566699}.
CC -!- INDUCTION: The trimeric FdhABC(3) complex is the main formate
CC dehydrogenase enzyme in the presence of molybdenum.
CC {ECO:0000269|PubMed:21498650}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC {ECO:0000255|PROSITE-ProRule:PRU00648}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AE017285; AAS97284.1; -; Genomic_DNA.
DR RefSeq; WP_010940078.1; NC_002937.3.
DR RefSeq; YP_012024.1; NC_002937.3.
DR STRING; 882.DVU_2812; -.
DR PaxDb; Q727P3; -.
DR PRIDE; Q727P3; -.
DR KEGG; dvu:DVU_2812; -.
DR PATRIC; fig|882.5.peg.2544; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_1_2_7; -.
DR OMA; HQQNWHT; -.
DR PhylomeDB; Q727P3; -.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0009326; C:formate dehydrogenase complex; IDA:UniProtKB.
DR GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0047111; F:formate dehydrogenase (cytochrome-c-553) activity; IDA:UniProtKB.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0045333; P:cellular respiration; IEA:InterPro.
DR GO; GO:0018291; P:molybdenum incorporation into iron-sulfur cluster; IDA:UniProtKB.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006443; Formate-DH-alph_fdnG.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR01553; formate-DH-alph; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Calcium; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Oxidoreductase; Periplasm; Reference proteome;
KW Selenium; Selenocysteine; Signal; Transport; Tungsten.
FT SIGNAL 1..33
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:21498650, ECO:0000269|PubMed:8566699"
FT CHAIN 34..1012
FT /note="Formate dehydrogenase 2 subunit alpha (cytochrome c-
FT 553)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000305|PubMed:21498650"
FT /id="PRO_0000430780"
FT DOMAIN 43..99
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q934F5,
FT ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q934F5,
FT ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 57
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q934F5,
FT ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 85
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q934F5,
FT ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 189
FT /ligand="W-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60537"
FT /ligand_part="W"
FT /ligand_part_id="ChEBI:CHEBI:27998"
FT /evidence="ECO:0000250|UniProtKB:Q934F5"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q934F5"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q934F5"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q934F5"
FT BINDING 424
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q934F5"
FT BINDING 426
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q934F5"
FT NON_STD 189
FT /note="Selenocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q934F5"
FT CONFLICT 40..41
FT /note="IE -> AI (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305|PubMed:8566699"
FT CONFLICT 44..45
FT /note="KE -> NT (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305|PubMed:8566699"
SQ SEQUENCE 1012 AA; 113389 MW; B08831962B834A41 CRC64;
MKTTRRSFLK LVGVSVVGLS LGQLGFDLED AQAYAVKLKI EGAKEVGTVC PFCSVCCQVI
AYVRNGKLVS TEGDPDFPVN EGALCAKGAA LFSMYTNPHR LTKPLYRAPH SDKWVEKDWD
WTLNQIARRV KDARDKDMIL KNDKGQTVNR LESIFMMGTS HASNEECAVI HQAMRGLGVV
HMDHQARVUH SPTVAALAES FGRGAMTNHW IDIKNTDAVL IIGSNAAEHH PVAFKWIMRA
RDNGAVLMHV DPKFSRTSAR CDFHVPLRSG TDIAFLGGMV NHIIAKDLYF KDYVANYTNA
AFVVGKDYAF EDGIFSGYDP KTRTYDRSKW EFEKGPDGGP VMDPTLKNER CVFNLMKKHY
ERYTLKNVSD VTGVSEENLL RVYDAFCATG RPDKAGTILY ALGWTQHTVG VQNIRTSTLI
QLLLGNIGVA GGGINALRGE PNVQGSTDHA LLYHILPGYN AMPVAQWQTL ADYNKANTPV
TTLKNSANWW SNRPKYVASL LKGWFGDAAT PENDFCYEYL PKLEKGEDYS YMYVMDRMYH
GKLKGGFIFG VNPMNSFPNT NKMRAALDKL DWLVCSELHN SETTDNWKRP GVDPKACKTE
VFLLPSAHRV EKAGTISNSG RWLQWFDKAV EPGQARNFAD IFVPLVNKIR ALYKAEGGTL
PDPVLKLHWT DKFDPEEWTR RINGFFWADT KVGDKEYKRG QLVPAFGQLK DDGSTSSLNW
LYTGSYTEED GNKSKRRDAR QTPMQANIGL FPNWSWCWPV NRRILYNRAS VDVNGKPWNP
KKAVIEWDGA KWVGDVPDGP WPPMADKEKG KLPFIMNKDG FAQFYGTGRM DGPFPEHYEP
AETPLDSHPF SKQLSSPVYK FHTSDMDQIA KAADPKYPIV LTTYSLTEHW CGGGETRNVP
NLLETEPQLY IEMSPELAEE KGIKNGDGVI VESIRGRAEA IAMVTVRIRP FTVMGKTVHL
VGMPFAYGWT TPKCGDSTNR LTVGAYDPNT TIPESKACLV NVRKADKLTE IA
