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Database: UniProt
Entry: A0A0L6U0Q4_9FIRM
LinkDB: A0A0L6U0Q4_9FIRM
Original site: A0A0L6U0Q4_9FIRM 
ID   A0A0L6U0Q4_9FIRM        Unreviewed;       551 AA.
AC   A0A0L6U0Q4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KNZ42088.1};
GN   ORFNames=AKG39_07905 {ECO:0000313|EMBL:KNZ42088.1};
OS   Acetobacterium bakii.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Acetobacterium.
OX   NCBI_TaxID=52689 {ECO:0000313|EMBL:KNZ42088.1, ECO:0000313|Proteomes:UP000036873};
RN   [1] {ECO:0000313|Proteomes:UP000036873}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8239 {ECO:0000313|Proteomes:UP000036873};
RA   Song Y., Hwang S., Cho B.-K.;
RT   "Draft genome sequence of Acetobacterium bakii DSM 8293, a potential
RT   psychrophilic chemical producer through syngas fermentation.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the SsuE family. Isf subfamily.
CC       {ECO:0000256|ARBA:ARBA00038292}.
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:KNZ42088.1}.
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DR   EMBL; LGYO01000019; KNZ42088.1; -; Genomic_DNA.
DR   RefSeq; WP_050739846.1; NZ_UOGO01000001.1.
DR   AlphaFoldDB; A0A0L6U0Q4; -.
DR   STRING; 52689.AKG39_07905; -.
DR   OrthoDB; 9805976at2; -.
DR   Proteomes; UP000036873; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.30.1050.10; SCP2 sterol-binding domain; 1.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR005025; FMN_Rdtase-like.
DR   InterPro; IPR003033; SCP2_sterol-bd_dom.
DR   InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR   PANTHER; PTHR43278:SF1; IRON-SULFUR FLAVOPROTEIN MJ1083; 1.
DR   PANTHER; PTHR43278; NAD(P)H-DEPENDENT FMN-CONTAINING OXIDOREDUCTASE YWQN-RELATED; 1.
DR   Pfam; PF03358; FMN_red; 1.
DR   Pfam; PF02036; SCP2; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF55718; SCP-like; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643}; Iron {ECO:0000256|ARBA:ARBA00022485};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036873};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        394..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        422..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        446..472
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        493..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        519..540
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          3..106
FT                   /note="NADPH-dependent FMN reductase-like"
FT                   /evidence="ECO:0000259|Pfam:PF03358"
FT   DOMAIN          268..346
FT                   /note="SCP2"
FT                   /evidence="ECO:0000259|Pfam:PF02036"
SQ   SEQUENCE   551 AA;  62455 MW;  2422B2DB11F97EB6 CRC64;
     MHNILVLNGS PKNNQSFTMK LVERFLSGVS DIAQDVKIET INLNEKNINP CTGCFGCWTI
     TPGQCVQEDD MDELLPMYEE ADIVIWATPL YHYGITSSMK KFMERTLPVF LPFIDPEGGG
     MYGHPYRNPE KMTDKKHILI STCGFPSVEN NYEGVEKQFD NLFGLGKWEK ILCVEGELLG
     ISQLDNFTGP YLELVKVAGR EYIDRLSISD SIKEGLTKPF VDIPAFLEVS NLSWGVEDIR
     EAESDGGLIA WSFMKQMRAA FNPKIRPGLD AVLQMDFTDL KESYQLVIND DQCTLLKNDF
     TQETTRITTH FTNWERLLEG KIDAAEALIE KKYMVAGDFD LMNALMDGLF GNLALFPEKQ
     KKLIPVVFKN TPYWFILTMI PWLACFFITE NNPFLGVIVP LLVSGILCSI KKGSELVYFD
     KATLLFFSVF TLITVPWSIG YNSVTIAFSA FMALFVIWMV SAFKTVPLTA DYTHFFSGRN
     ALKNILFLKT NRILTVIWAL LFLIQGGIAL WLTSTAMESY AAILPQLLLI PGVFFSVWFI
     NWYPAYSAKT E
//
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