CYSD_ALLVD
ID CYSD_ALLVD Reviewed; 199 AA.
AC Q06529; D3RRX8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Cytochrome subunit of sulfide dehydrogenase;
DE AltName: Full=FCSD;
DE Short=FC;
DE AltName: Full=Flavocytochrome c cytochrome subunit;
DE Flags: Precursor;
GN Name=fccA; OrderedLocusNames=Alvin_1093;
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8390993; DOI=10.1016/s0021-9258(19)85257-2;
RA Dolata M.M., van Beeumen J.J., Ambler R.P., Meyer T.E., Cusanovich M.A.;
RT "Nucleotide sequence of the heme subunit of flavocytochrome c from the
RT purple phototrophic bacterium, Chromatium vinosum. A 2.6-kilobase pair DNA
RT fragment contains two multiheme cytochromes, a flavoprotein, and a homolog
RT of human ankyrin.";
RL J. Biol. Chem. 268:14426-14431(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(2011).
RN [3]
RP PROTEIN SEQUENCE OF 26-199.
RX PubMed=1649169; DOI=10.1016/s0021-9258(18)98783-1;
RA van Beeumen J.J., Demol H., Samyn B., Bartsch R.G., Meyer T.E.,
RA Dolata M.M., Cusanovich M.A.;
RT "Covalent structure of the diheme cytochrome subunit and amino-terminal
RT sequence of the flavoprotein subunit of flavocytochrome c from Chromatium
RT vinosum.";
RL J. Biol. Chem. 266:12921-12931(1991).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=7939681; DOI=10.1126/science.7939681;
RA Chen Z.-W., Koh M., van Driessche G., van Beeumen J.J., Bartsch R.G.,
RA Meyer T.E., Cusanovich M.A., Mathews F.S.;
RT "The structure of flavocytochrome c sulfide dehydrogenase from a purple
RT phototrophic bacterium.";
RL Science 266:430-432(1994).
CC -!- FUNCTION: Diheme cytochrome that function as the electron transport
CC subunit of sulfide dehydrogenase.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is about +15 mV.;
CC -!- SUBUNIT: Dimer of one cytochrome and one flavoprotein.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Binds 2 heme c groups covalently per subunit.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L13419; AAA23316.1; -; Genomic_DNA.
DR EMBL; CP001896; ADC62032.1; -; Genomic_DNA.
DR PIR; C47169; C47169.
DR RefSeq; WP_012970308.1; NC_013851.1.
DR PDB; 1FCD; X-ray; 2.53 A; C/D=26-199.
DR PDBsum; 1FCD; -.
DR AlphaFoldDB; Q06529; -.
DR SMR; Q06529; -.
DR DIP; DIP-6170N; -.
DR STRING; 572477.Alvin_1093; -.
DR EnsemblBacteria; ADC62032; ADC62032; Alvin_1093.
DR KEGG; alv:Alvin_1093; -.
DR eggNOG; COG2863; Bacteria.
DR HOGENOM; CLU_076280_3_2_6; -.
DR OMA; HLKSCES; -.
DR OrthoDB; 1853490at2; -.
DR BioCyc; MetaCyc:MON-12316; -.
DR EvolutionaryTrace; Q06529; -.
DR Proteomes; UP000001441; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR Gene3D; 1.10.760.10; -; 2.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR024167; Cytochrome_c4-like.
DR PIRSF; PIRSF000005; Cytochrome_c4; 1.
DR SUPFAM; SSF46626; SSF46626; 2.
DR PROSITE; PS51007; CYTC; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW Metal-binding; Periplasm; Reference proteome; Signal; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:1649169"
FT CHAIN 26..199
FT /note="Cytochrome subunit of sulfide dehydrogenase"
FT /id="PRO_0000006569"
FT BINDING 36
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 39
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 40
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:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 79
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:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 126
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 129
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 130
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:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 168
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:0000255|PROSITE-ProRule:PRU00433"
FT HELIX 29..34
FT /evidence="ECO:0007829|PDB:1FCD"
FT TURN 35..39
FT /evidence="ECO:0007829|PDB:1FCD"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:1FCD"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:1FCD"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:1FCD"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:1FCD"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:1FCD"
FT TURN 126..129
FT /evidence="ECO:0007829|PDB:1FCD"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1FCD"
FT HELIX 151..162
FT /evidence="ECO:0007829|PDB:1FCD"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:1FCD"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1FCD"
FT HELIX 185..197
FT /evidence="ECO:0007829|PDB:1FCD"
SQ SEQUENCE 199 AA; 21636 MW; F8D50A84F93A4AFC CRC64;
MTQSTPRLML AASVLALGLA SNAGAEPTAE MLTNNCAGCH GTHGNSVGPA SPSIAQMDPM
VFVEVMEGFK SGEIASTIMG RIAKGYSTAD FEKMAGYFKQ QTYQPAKQSF DTALADTGAK
LHDKYCEKCH VEGGKPLADE EDYHILAGQW TPYLQYAMSD FREERRPMEK KMASKLRELL
KAEGDAGLDA LFAFYASQQ
