ID A0A0Q8RQK1_9BURK Unreviewed; 421 AA.
AC A0A0Q8RQK1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Flavocytochrome C {ECO:0000313|EMBL:KRB97022.1};
GN ORFNames=ASE26_03010 {ECO:0000313|EMBL:KRB97022.1};
OS Duganella sp. Root198D2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1736489 {ECO:0000313|EMBL:KRB97022.1, ECO:0000313|Proteomes:UP000051728};
RN [1] {ECO:0000313|EMBL:KRB97022.1, ECO:0000313|Proteomes:UP000051728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root198D2 {ECO:0000313|EMBL:KRB97022.1,
RC ECO:0000313|Proteomes:UP000051728};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB97022.1, ECO:0000313|Proteomes:UP000051728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root198D2 {ECO:0000313|EMBL:KRB97022.1,
RC ECO:0000313|Proteomes:UP000051728};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KRB97022.1}.
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DR EMBL; LMIC01000012; KRB97022.1; -; Genomic_DNA.
DR RefSeq; WP_055938686.1; NZ_LMIC01000012.1.
DR AlphaFoldDB; A0A0Q8RQK1; -.
DR Proteomes; UP000051728; 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 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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000051728}.
FT DOMAIN 29..152
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 162..276
FT /note="Sulfide dehydrogenase [flavocytochrome c]
FT flavoprotein chain central"
FT /evidence="ECO:0000259|Pfam:PF21706"
FT DOMAIN 355..420
FT /note="Flavocytochrome c sulphide dehydrogenase flavin-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF09242"
SQ SEQUENCE 421 AA; 45405 MW; A31E9C428558864B CRC64;
MERRTFVQAA AILAATTGCA SIGGRAQAHV VVVGGGYGGA TAAKYVRLWS QGSIDVTLIE
PSANFVSCPL SNLVLGGSRQ LQDLTRSYDD LQRKHGVKIL HDSASSIDPE KRTIKLLSGE
VLSYDRLILS PGIEFLWSEL PGMSVEGAQD KILHAWKAGP QTTALRAQLE AMHDGGVFAM
TVPPAPYRCP PGPYERVCQV AHYFSQHKPK SKVLLLDANE DVVSKGPLFK KVWKERYASI
IEYRPSFKTV DVDVAARTAV SELGDKVKAD VLNVVPPQRA GAIAAQTGLA NMNKRWCEVD
FITFESTQAK NIHVIGDAIQ GSPLMPKSGH MANQHAKVCA AAVVDLLSGR APEQSPLLTN
TCYSYVSDKD VIHVASVHAY NAEKKTLLVV PGSGGVSPGP TELEGHYANS WAQNIWNDIL
S
//
