ID E1QIX2_DESB2 Unreviewed; 1011 AA.
AC E1QIX2;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:ADK85515.1};
GN OrderedLocusNames=Deba_2150 {ECO:0000313|EMBL:ADK85515.1};
OS Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802
OS / 2st14).
OC Bacteria; Thermodesulfobacteriota; Desulfarculia; Desulfarculales;
OC Desulfarculaceae; Desulfarculus.
OX NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK85515.1, ECO:0000313|Proteomes:UP000009047};
RN [1] {ECO:0000313|EMBL:ADK85515.1, ECO:0000313|Proteomes:UP000009047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802 / 2st14
RC {ECO:0000313|Proteomes:UP000009047};
RX PubMed=21304732; DOI=10.4056/sigs.1243258;
RA Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G., Pati A.,
RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Han C., Rohde M., Brambilla E., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Land M.;
RT "Complete genome sequence of Desulfarculus baarsii type strain (2st14).";
RL Stand. Genomic Sci. 3:276-284(2010).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the HdrA family.
CC {ECO:0000256|ARBA:ARBA00006561}.
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DR EMBL; CP002085; ADK85515.1; -; Genomic_DNA.
DR RefSeq; WP_013258956.1; NC_014365.1.
DR AlphaFoldDB; E1QIX2; -.
DR STRING; 644282.Deba_2150; -.
DR KEGG; dbr:Deba_2150; -.
DR eggNOG; COG1148; Bacteria.
DR HOGENOM; CLU_004231_2_0_7; -.
DR OrthoDB; 9766627at2; -.
DR Proteomes; UP000009047; Chromosome.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR039650; HdrA-like.
DR PANTHER; PTHR43498:SF1; COB--COM HETERODISULFIDE REDUCTASE IRON-SULFUR SUBUNIT A; 1.
DR PANTHER; PTHR43498; FERREDOXIN:COB-COM HETERODISULFIDE REDUCTASE SUBUNIT A; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF12831; FAD_oxidored; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000009047}.
FT DOMAIN 104..133
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 935..964
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 965..994
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1011 AA; 107710 MW; C92E66F0EE010BE0 CRC64;
MSDATQKGRL ETVLVIGGGI AGLKSALDLA ESGRQVVVTD KAPNLGGYLP LLDRQFPTND
CQICYLSPDM APAGFDIGIG VMPLTEVVGV SGQAGDFTVE LTTKPRYIDT ELCTACGECL
KAAPEGAVSF TPGLDHRSTT CLRYPQAVPQ AFAINIDKVG QDTSWIKCCE PGAIKLDQKP
ESVKLNVGSI IVATGAELFD PTPLSDYFGY GQFPDVVTSL EFERILSPAG PTCGAFARPS
DGRRPTRIGW VQCVGSRTTK APGNPYCSSI CCMFAMKEAA WAKEHFASDL DATIFYMDIR
PMGKDYEQYY QRMKNDVGVN FVRCRPHTVR RDEATNDLLL SYATEDGQQL EAALDMLVLA
TGFCASKEAV STAQALGIEL DKYNFVKVSD KAPVSTSREG VYACGMSTGP KDIPDSLMQA
SAAACLASAH LTPPEPVRYE KDLPPERDTA SETPKIGVFV ADFGGNMAKY VDLAKVMAAA
KTMPNVCCVE EIKVSYAGGQ GLTQMIDSIK ASGVNRVVVV GNSPRTHGKI YAEAVRRAGL
NRAMVEIANV RDQDALVHRD APEAATHKAI MLVRMAVGRV KLAKPIYVHA QSLDKTALVV
GGGVAGLTAA LQLAKQGISV KLVERDKQLG GMALNLAHTL GGEPVRPIVE ELVAQVQASD
KIEVILDALV VDHKGCVGDF TTGVQSGPAM YYQQIKHGVT IIATGGKAYK PEGYFYGKNP
AVMTQVELGV KLAAGQTDGL DTVVMIQCVG SRNDANPACG RICCRSAVLN ALEIKRKKPE
ATVVVLYRDM RTPYDSEDNY RLARELGVLF ARYEAGQPPK VADNGATMLV EFDDPILGRT
VDVEATALVL STPQVADEEG LEDLCDIFKL QQTETGFLLE EHVKVRPVDT PEPGVFAAGS
VLAPKSIDEA ITQGAAAAGR AITVLAQESV QVSGGVAKVV GEMCAACLVC VRACPIGVPF
INADGYSQID PEKCLGCGIC AAECPAKAIQ LQGYDDDQIM GQTDALLEGV L
//
