FDNGB_DESVH
ID FDNGB_DESVH Reviewed; 219 AA.
AC Q727P4;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Formate dehydrogenase 2 subunit beta (cytochrome c-553) {ECO:0000303|PubMed:16274230};
DE Short=FDH2 subunit beta (cytochrome c-553) {ECO:0000303|PubMed:16274230};
DE AltName: Full=Formate dehydrogenase small subunit (cytochrome c-553);
GN OrderedLocusNames=DVU_2811 {ECO:0000312|EMBL:AAS97283.1};
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 2-21, 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 [3]
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).
RN [4]
RP SUBUNIT, INDUCTION BY MOLYBDENUM, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
CC -!- FUNCTION: Beta chain of the formate dehydrogenase (FDH) that catalyzes
CC the reversible two-electron oxidation of formate to carbon dioxide. The
CC beta chain is an electron transfer unit. {ECO:0000269|PubMed:8566699}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q8GC87};
CC Note=Binds 3 [4Fe-4S] clusters. {ECO:0000250|UniProtKB:Q8GC87};
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}.
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DR EMBL; AE017285; AAS97283.1; -; Genomic_DNA.
DR RefSeq; WP_010940077.1; NC_002937.3.
DR RefSeq; YP_012023.1; NC_002937.3.
DR AlphaFoldDB; Q727P4; -.
DR SMR; Q727P4; -.
DR STRING; 882.DVU_2811; -.
DR PaxDb; Q727P4; -.
DR EnsemblBacteria; AAS97283; AAS97283; DVU_2811.
DR KEGG; dvu:DVU_2811; -.
DR PATRIC; fig|882.5.peg.2543; -.
DR eggNOG; COG0437; Bacteria.
DR HOGENOM; CLU_043374_0_3_7; -.
DR OMA; FWGSIGA; -.
DR PhylomeDB; Q727P4; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR Pfam; PF13247; Fer4_11; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Periplasm; Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8566699"
FT CHAIN 2..219
FT /note="Formate dehydrogenase 2 subunit beta (cytochrome c-
FT 553)"
FT /id="PRO_0000430781"
FT DOMAIN 3..32
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000250|UniProtKB:Q8GC87,
FT ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 132..171
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000250|UniProtKB:Q8GC87"
FT BINDING 12
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GC87"
FT BINDING 15
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GC87"
FT BINDING 18
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GC87"
FT BINDING 22
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GC87"
FT BINDING 74
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q8GC87"
FT BINDING 77
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q8GC87"
FT BINDING 82
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q8GC87"
FT BINDING 124
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q8GC87"
FT BINDING 141
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GC87"
FT BINDING 144
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GC87"
FT BINDING 156
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GC87"
FT BINDING 160
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GC87"
SQ SEQUENCE 219 AA; 24470 MW; 69994768416A6025 CRC64;
MPKAFLIDTT RCTACRGCQL ACKEWHDLPA NVTKQRGSHQ NPPDLNPNNL KIVRFNERMN
EKGVVIWNFF PDQCRHCVTP VCVDVADMAV PGAMIKDKKT GAVLATEKSA KLSPADAKAV
AEACPYNIPR IDPKTKRITK CDMCFDRVSA GMQPICVKTC PTGTMAFGER DEMLALAEKR
LADAKTRFPK AHLVDVEDVS VIYLLAEEKE HYYEYAGFM
