DHSU_ALLVD
ID DHSU_ALLVD Reviewed; 431 AA.
AC Q06530; D3RRX7; O31157;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Sulfide dehydrogenase [flavocytochrome c] flavoprotein chain;
DE EC=1.8.2.3;
DE AltName: Full=FCSD;
DE AltName: Full=Flavocytochrome c flavoprotein subunit;
DE Short=FC;
DE Flags: Precursor;
GN Name=fccB; OrderedLocusNames=Alvin_1092;
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].
RA Reinartz M., Trueper H.G., Dahl C.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125, AND PROTEIN SEQUENCE OF 31-86;
RP 90-114 AND 119-125.
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 [4]
RP PROTEIN SEQUENCE OF 31-78.
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 [5]
RP CATALYTIC ACTIVITY.
RX PubMed=222744; DOI=10.1093/oxfordjournals.jbchem.a132467;
RA Fukumori Y., Yamanaka T.;
RT "Flavocytochrome c of Chromatium vinosum. Some enzymatic properties and
RT subunit structure.";
RL J. Biochem. 85:1405-1414(1979).
RN [6]
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 -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome c] + hydrogen sulfide = 2 Fe(II)-
CC [cytochrome c] + H(+) + sulfur; Xref=Rhea:RHEA:30223, Rhea:RHEA-
CC COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:26833, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:29919; EC=1.8.2.3; Evidence={ECO:0000269|PubMed:222744};
CC -!- SUBUNIT: Dimer of one cytochrome and one flavoprotein.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
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DR EMBL; AF031149; AAB86576.1; -; Genomic_DNA.
DR EMBL; CP001896; ADC62031.1; -; Genomic_DNA.
DR EMBL; L13419; AAA23317.1; -; Genomic_DNA.
DR RefSeq; WP_012970307.1; NC_013851.1.
DR PDB; 1FCD; X-ray; 2.53 A; A/B=31-431.
DR PDBsum; 1FCD; -.
DR AlphaFoldDB; Q06530; -.
DR SMR; Q06530; -.
DR DIP; DIP-6169N; -.
DR STRING; 572477.Alvin_1092; -.
DR EnsemblBacteria; ADC62031; ADC62031; Alvin_1092.
DR KEGG; alv:Alvin_1092; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_030742_0_0_6; -.
DR OMA; GWCPCDA; -.
DR OrthoDB; 403436at2; -.
DR BioCyc; MetaCyc:MON-12317; -.
DR EvolutionaryTrace; Q06530; -.
DR Proteomes; UP000001441; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0070225; F:sulfide dehydrogenase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.50.50.60; -; 2.
DR Gene3D; 3.90.760.10; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR015323; FlavoCytC_S_DH_flav-bd.
DR InterPro; IPR037092; FlavoCytC_S_DH_flav-bd_sf.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR Pfam; PF09242; FCSD-flav_bind; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF10518; TAT_signal; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
DR SUPFAM; SSF55424; SSF55424; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
KW Oxidoreductase; Periplasm; Redox-active center; Reference proteome; Signal.
FT SIGNAL 1..30
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:1649169, ECO:0000269|PubMed:8390993"
FT CHAIN 31..431
FT /note="Sulfide dehydrogenase [flavocytochrome c]
FT flavoprotein chain"
FT /id="PRO_0000021105"
FT BINDING 70..76
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT DISULFID 191..367
FT /note="Redox-active"
FT CONFLICT 68
FT /note="D -> K (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:1FCD"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:1FCD"
FT HELIX 75..79
FT /evidence="ECO:0007829|PDB:1FCD"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:1FCD"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:1FCD"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1FCD"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:1FCD"
FT TURN 148..153
FT /evidence="ECO:0007829|PDB:1FCD"
FT HELIX 162..173
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:1FCD"
FT HELIX 194..206
FT /evidence="ECO:0007829|PDB:1FCD"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:1FCD"
FT HELIX 227..238
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:1FCD"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:1FCD"
FT HELIX 290..294
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:1FCD"
FT HELIX 335..354
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 363..372
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 375..385
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:1FCD"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:1FCD"
FT HELIX 408..428
FT /evidence="ECO:0007829|PDB:1FCD"
SQ SEQUENCE 431 AA; 45898 MW; 7F24AE33B83D89BF CRC64;
MTLNRRDFIK TSGAAVAAVG ILGFPHLAFG AGRKVVVVGG GTGGATAAKY IKLADPSIEV
TLIEPNTDYY TCYLSNEVIG GDRKLESIKH GYDGLRAHGI QVVHDSATGI DPDKKLVKTA
GGAEFGYDRC VVAPGIELIY DKIEGYSEEA AAKLPHAWKA GEQTAILRKQ LEDMADGGTV
VIAPPAAPFR CPPGPYERAS QVAYYLKAHK PKSKVIILDS SQTFSKQSQF SKGWERLYGF
GTENAMIEWH PGPDSAVVKV DGGEMMVETA FGDEFKADVI NLIPPQRAGK IAQIAGLTND
AGWCPVDIKT FESSIHKGIH VIGDACIANP MPKSGYSANS QGKVAAAAVV ALLKGEEPGT
PSYLNTCYSI LAPAYGISVA AIYRPNADGS AIESVPDSGG VTPVDAPDWV LEREVQYAYS
WYNNIVHDTF G
