CYC32_DESVH
ID CYC32_DESVH Reviewed; 144 AA.
AC Q727P6;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Cytochrome c3 {ECO:0000303|PubMed:8566699};
DE AltName: Full=Formate dehydrogenase 2 subunit gamma (cytochrome c-553) {ECO:0000303|PubMed:16274230};
DE Short=FDH2 subunit gamma (cytochrome c-553) {ECO:0000303|PubMed:16274230};
DE Short=FDH2C {ECO:0000303|PubMed:16274230};
DE Flags: Precursor;
GN OrderedLocusNames=DVU_2809 {ECO:0000312|EMBL:AAS97281.1};
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 25-39, 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 PROTEIN SEQUENCE OF N-TERMINUS, 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: Participates in sulfate respiration coupled with
CC phosphorylation by transferring electrons from the enzyme dehydrogenase
CC to ferredoxin (By similarity). Gamma chain of the formate dehydrogenase
CC (FDH) that catalyzes the reversible two-electron oxidation of formate
CC to carbon dioxide. The gamma subunit of formate dehydrogenase forms a
CC c-type heme. {ECO:0000250|UniProtKB:P38554,
CC ECO:0000269|PubMed:8566699}.
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: Homodimer (By similarity). Heterotrimer of cytochrome c3 FDH2C
CC and formate dehydrogenase FDH2 alpha and beta subunits that forms the
CC FdhABC(3) complex. {ECO:0000250|UniProtKB:P38554,
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: Binds 4 heme c groups per subunit. {ECO:0000250|UniProtKB:P38554}.
CC -!- MISCELLANEOUS: The second heme binding site has an unusual CXXXXCH
CC motif. {ECO:0000250|UniProtKB:P00133}.
CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
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DR EMBL; AE017285; AAS97281.1; -; Genomic_DNA.
DR RefSeq; WP_010940075.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_012021.1; NC_002937.3.
DR AlphaFoldDB; Q727P6; -.
DR STRING; 882.DVU_2809; -.
DR PaxDb; Q727P6; -.
DR EnsemblBacteria; AAS97281; AAS97281; DVU_2809.
DR KEGG; dvu:DVU_2809; -.
DR PATRIC; fig|882.5.peg.2541; -.
DR eggNOG; ENOG5032JRW; Bacteria.
DR HOGENOM; CLU_125874_3_1_7; -.
DR OMA; RPCHMSP; -.
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:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009061; P:anaerobic respiration; IEA:UniProtKB-KW.
DR InterPro; IPR002322; Cyt_c_III.
DR InterPro; IPR020942; Cyt_c_III_dom.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR Pfam; PF02085; Cytochrom_CIII; 1.
DR PRINTS; PR00609; CYTOCHROMEC3.
DR SUPFAM; SSF48695; SSF48695; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW Periplasm; Reference proteome; Signal; Sulfate respiration; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:16274230,
FT ECO:0000269|PubMed:8566699"
FT CHAIN 25..144
FT /note="Cytochrome c3"
FT /id="PRO_0000430782"
FT BINDING 51
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P38554"
FT BINDING 54
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P38554"
FT BINDING 59
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P38554"
FT BINDING 62
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P38554"
FT BINDING 63
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P38554"
FT BINDING 64
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P38554"
FT BINDING 76
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P38554"
FT BINDING 81
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P38554"
FT BINDING 82
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P38554"
FT BINDING 100
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P38554"
FT BINDING 108
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P38554"
FT BINDING 111
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P38554"
FT BINDING 112
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P38554"
FT BINDING 125
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P00133"
FT BINDING 128
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P00133"
FT BINDING 129
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P38554"
SQ SEQUENCE 144 AA; 15873 MW; C25C58C557616C1C CRC64;
MRYLVISLFA VSLLMAGSAL VGNAADAAKA PKKAIELKHG TSKRMHVMFN HTTHKDIACE
QCHHDSPAPD KPYASCTDND CHATPGPRER DTMSMFVAYH AKDTDRSCYG CHKKMAAQHP
EFTGCRPCHM SQQARKEAAA SEKK
