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Database: UniProt
Entry: A0A1I0FIM6_9BACI
LinkDB: A0A1I0FIM6_9BACI
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ID   A0A1I0FIM6_9BACI        Unreviewed;       757 AA.
AC   A0A1I0FIM6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Alcohol dehydrogenase (Cytochrome c) {ECO:0000313|EMBL:SET57295.1};
GN   ORFNames=SAMN05216389_11540 {ECO:0000313|EMBL:SET57295.1};
OS   Oceanobacillus limi.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=930131 {ECO:0000313|EMBL:SET57295.1, ECO:0000313|Proteomes:UP000198618};
RN   [1] {ECO:0000313|EMBL:SET57295.1, ECO:0000313|Proteomes:UP000198618}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBRC-M 10780 {ECO:0000313|EMBL:SET57295.1,
RC   ECO:0000313|Proteomes:UP000198618};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC         Evidence={ECO:0000256|ARBA:ARBA00001931};
CC   -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00008156}.
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DR   EMBL; FOHE01000015; SET57295.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0FIM6; -.
DR   STRING; 930131.SAMN05216389_11540; -.
DR   OrthoDB; 9794322at2; -.
DR   Proteomes; UP000198618; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   Gene3D; 2.140.10.10; Quinoprotein alcohol dehydrogenase-like superfamily; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR008168; Cyt_C_IC.
DR   InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR   InterPro; IPR002372; PQQ_repeat.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   PANTHER; PTHR32303; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1.
DR   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   Pfam; PF13360; PQQ_2; 2.
DR   PRINTS; PR00605; CYTCHROMECIC.
DR   SMART; SM00564; PQQ; 6.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00433}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198618};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          678..754
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   REGION          32..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          650..680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..53
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   757 AA;  83600 MW;  61A01F435E7D5A64 CRC64;
     MEKLEKSMWI AIIAVVIITV GGYFVFQGTG NNDHAESPIE DTEQEDQEGE EQGDSGEGEA
     KENEDRSPSD HQSFQHMEYT GDIAPDFSAE ELTELPTNNW ITFGGNIYNG RYSPLNRVDE
     NNVAELKADW VTSLGSGFDF KYSGEATPLV YDGVMFTITG ANNVSALDAT TGEIIWEFRP
     KLPDDLDTLC CGWASRGVAL GDGKVYVALL DARLVALDQK TGEVVWETRV DEWEKGYTIT
     SAPLFYDGKV YTGIAGGEYG IRGYVAAYDA DLGRQIWRSY TIPAPGEPGH ETWPEDNDAW
     IKGGAPVWQT PAVDPELNMI YFATGNTSPD LDGSNREGDN LYADSMLALD ADTGEYQWHF
     QQVHHDIWDL DPANPVVLYD VEMDGEMKKG IAQAGKTGWV YMLDRTNGEP LIGIEEKEVP
     QNENQKTSPT QPFPEGDAFV PQEITEEDIE RDLPEDFEGE VGSIFTPFWD EPVTIKPSPQ
     GGGNWPPSAY NPDTELFYVL GNDNYFAYAH YAEDEANKFE EGKEWIGSIW QPISDAPFGG
     TVTALDIKTN RIVWQKEWDT IAYSGILTTK GNLVFVGHND GRIIAYNATT GDQVWEFMTD
     AGANAPPITY EVDGKQYVSI FSAGNSLAGT KHGDKIYTFS LDGEFESLED ISDEDINRSP
     IQSDEAEEAE EQNESQGSAV ENGQKVYENN CLACHGAEGV GGHNGPNLQN SPMLDDDDSL
     IQQILHGSGA MPGFEDSLDE DEINALVEYL KSLKNEE
//
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