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Database: UniProt
Entry: K0NP93_DESTT
LinkDB: K0NP93_DESTT
Original site: K0NP93_DESTT 
ID   K0NP93_DESTT            Unreviewed;       971 AA.
AC   K0NP93;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=BamE3: predicted heterodisulfide reductase, iron-sulfur subunit A {ECO:0000313|EMBL:CCK82510.1};
GN   Name=bamE3 {ECO:0000313|EMBL:CCK82510.1};
GN   OrderedLocusNames=TOL2_C43540 {ECO:0000313|EMBL:CCK82510.1};
OS   Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfobacula.
OX   NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK82510.1, ECO:0000313|Proteomes:UP000007347};
RN   [1] {ECO:0000313|EMBL:CCK82510.1, ECO:0000313|Proteomes:UP000007347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX   PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA   Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA   Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT   "Complete genome, catabolic sub-proteomes and key-metabolites of
RT   Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT   sulfate-reducing bacterium.";
RL   Environ. Microbiol. 15:1334-55(2013).
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; FO203503; CCK82510.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0NP93; -.
DR   STRING; 651182.TOL2_C43540; -.
DR   KEGG; dto:TOL2_C43540; -.
DR   PATRIC; fig|651182.5.peg.5123; -.
DR   HOGENOM; CLU_004231_2_0_7; -.
DR   Proteomes; UP000007347; 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   Gene3D; 3.30.70.20; -; 2.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
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; PF00037; Fer4; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000007347}.
FT   DOMAIN          22..53
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          860..889
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          893..922
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   971 AA;  107579 MW;  E5F56335C0E37AC4 CRC64;
     MTFTEVEKVE GEKGDFQVSL KTRPRYIIEE KCTGCTTCME YCPKEYPDQF NQGISQNKAV
     HVYFSQAIPL VAYIDDSCLF LKEEKCDICR GVCQADAIDF NQTPKKTDIN VGAIILSSGI
     TPFDPSVKDE YGYRKMQNVV TSMDYERLLS STGPYEGQVL RASDKKHPKK IAWIQCVGSR
     RVTEGDNSYC SGVCCTYTQK QVILTKHHYD DAECTIFHND IRSFGKDFER YFQRAEQLDG
     VEFIRSYASV TRENPETKNV AVRYATTDEG VKEEEFDMVV LSVGLNPPAA YKELSDMFGI
     DLNSHGFCES DSSNPIKTSR PGIFVSGAFQ GPTDIPESVF TASGAGSQIG EMLDYRRGNL
     AKERIYPVER DVSGEEPRIG VFVCHCGANI SSVVNVPSTV EYALTLPNVV YAKEQIFSCA
     TNSAKEITDL AKEKGLNRVV IAACSPRTLE PLFRDTLREA GLNQYYLDMA NIREHCSWVH
     TKQKEEATQK AQDIVRMSVA RASQLEPLKE FDLPVNKAAL VVGGGIAGMT CALSIAAQGH
     EVHLVEKSKD LGGMARRIYS TLEGLDVQTY LDNVIQQVYK NPLIHVSHEA VIKDVSGYLG
     NFTTTLETEG RSKVIKHGAS VLAIGADVYK PTEYLYGEND AVFTHLELGE EIAKANPAVV
     NAESLVMIQC VGCRNEDRNY CSRVCCGHAV KNALKLKEKN PDMRIYILFR DMRTYGFRED
     AYREASENDV RFIRYTPEDK PVVQTAKEGG KDIIRVTVPD PILGQRLELD ADVLSLAAAV
     IPTESTEEIA GHFKVTLSPD EFFKEAHVKL KPVEFATDGV FLCGTAHYPK HIPETINQAY
     GAAGRVLTLL SRDTVVASGS VAKVNEYDCV SCGACITACT YDAIEFRDTP KGKKAWVNPI
     LCKGDGLCNA KCPTNAIVLK HFTNDALFNQ IDAAITKEDI IEQMDSVLEQ VDTAAAKEDV
     IEQMDAVLEN V
//
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