ID A0A0Q2YWA2_9RHOB Unreviewed; 422 AA.
AC A0A0Q2YWA2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Flavocytochrome C {ECO:0000313|EMBL:KQI67412.1};
GN ORFNames=AN189_15850 {ECO:0000313|EMBL:KQI67412.1};
OS Loktanella sp. 3ANDIMAR09.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Loktanella.
OX NCBI_TaxID=1225657 {ECO:0000313|EMBL:KQI67412.1, ECO:0000313|Proteomes:UP000051463};
RN [1] {ECO:0000313|EMBL:KQI67412.1, ECO:0000313|Proteomes:UP000051463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3ANDIMAR09 {ECO:0000313|EMBL:KQI67412.1,
RC ECO:0000313|Proteomes:UP000051463};
RA Mas-Llado M., Nogales B., Bosch R.;
RT "Draft genome sequence of Loktanella sp. 3ANDIMAR09.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQI67412.1}.
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; LJAK01000013; KQI67412.1; -; Genomic_DNA.
DR RefSeq; WP_056038077.1; NZ_LJAK01000013.1.
DR AlphaFoldDB; A0A0Q2YWA2; -.
DR STRING; 1225657.AN189_15850; -.
DR PATRIC; fig|1225657.3.peg.3261; -.
DR OrthoDB; 9802771at2; -.
DR Proteomes; UP000051463; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.90.760.10; Flavocytochrome c sulphide dehydrogenase, flavin-binding domain; 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; IPR049386; FCSD_central.
DR InterPro; IPR015323; FlavoCytC_S_DH_flav-bd.
DR InterPro; IPR037092; FlavoCytC_S_DH_flav-bd_sf.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43755; -; 1.
DR PANTHER; PTHR43755:SF1; POSSIBLE DEHYDROGENASE_REDUCTASE; 1.
DR Pfam; PF09242; FCSD-flav_bind; 1.
DR Pfam; PF21706; FCSD_central; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000051463};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..422
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006200474"
FT DOMAIN 31..144
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 163..278
FT /note="Sulfide dehydrogenase [flavocytochrome c]
FT flavoprotein chain central"
FT /evidence="ECO:0000259|Pfam:PF21706"
FT DOMAIN 354..419
FT /note="Flavocytochrome c sulphide dehydrogenase flavin-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF09242"
SQ SEQUENCE 422 AA; 44544 MW; EA928AE18DFC0409 CRC64;
MTLNRRLFLG SSIAAAGALA APMVRAQGKP RVVVVGGGAG GATAARYIAK DSDGAIDVTL
IEPSRTYYTC FFSNLYIGGL RDLQSIAHSY GTLASAFGIN VVHDWVIGVD RDAKTVALAS
GGSLPYDRLI LSPGIDFIDD AVPGWSVASQ NAMPHAYKGG SQTELLKAQV EAMPQGGTFA
MIAPPNPYRC PPGPYERVSM VAHKLKAENP TAKILILDPK EGFSKQALFV EGWQKHYPGM
IERIGPDFGG GNVSVNPDEM TVDIDGDVQK VDVCNVIPAQ KAGLIAEAAG LTEGNWAPVN
PTDLSSTMDE NIHVLGDAAA QGAMPKSGFA ANSQAKVCAN AVRGALTGST VFPARFSNTC
WSLIDTDDGV KVGATYEAGE TEIVALDTFV SQTNETAEVR EETYDESVGW YQAITEDMFG
QA
//
