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Database: UniProt
Entry: F7PFC0_9EURY
LinkDB: F7PFC0_9EURY
Original site: F7PFC0_9EURY 
ID   F7PFC0_9EURY            Unreviewed;       553 AA.
AC   F7PFC0;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   SubName: Full=D-sorbitol dehydrogenase protein {ECO:0000313|EMBL:ERJ05750.1};
DE            EC=1.1.99.21 {ECO:0000313|EMBL:ERJ05750.1};
DE   SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:CCQ33926.1};
GN   ORFNames=HLRTI_002277 {ECO:0000313|EMBL:ERJ05750.1}, HTIA_1802
GN   {ECO:0000313|EMBL:CCQ33926.1};
OS   Halorhabdus tiamatea SARL4B.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halorhabdus.
OX   NCBI_TaxID=1033806 {ECO:0000313|EMBL:ERJ05750.1, ECO:0000313|Proteomes:UP000003861};
RN   [1] {ECO:0000313|EMBL:ERJ05750.1, ECO:0000313|Proteomes:UP000003861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARL4B {ECO:0000313|EMBL:ERJ05750.1,
RC   ECO:0000313|Proteomes:UP000003861};
RX   PubMed=21705593; DOI=10.1128/JB.05462-11;
RA   Antunes A., Alam I., Bajic V.B., Stingl U.;
RT   "Genome sequence of Halorhabdus tiamatea, the first archaeon isolated from
RT   a deep-sea anoxic brine lake.";
RL   J. Bacteriol. 193:4553-4554(2011).
RN   [2] {ECO:0000313|EMBL:ERJ05750.1, ECO:0000313|Proteomes:UP000003861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARL4B {ECO:0000313|EMBL:ERJ05750.1,
RC   ECO:0000313|Proteomes:UP000003861};
RX   PubMed=24324765;
RA   Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U.,
RA   Bajic V.B.;
RT   "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples from
RT   the Red Sea Extremophiles.";
RL   PLoS ONE 8:E82210-E82210(2013).
RN   [3] {ECO:0000313|EMBL:CCQ33926.1, ECO:0000313|Proteomes:UP000015381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARL4B {ECO:0000313|Proteomes:UP000015381}, and Type strain:
RC   SARL4B {ECO:0000313|EMBL:CCQ33926.1};
RX   PubMed=24428220; DOI=10.1111/1462-2920.12393;
RA   Werner J., Ferrer M., Michel G., Mann A.J., Huang S., Juarez S.,
RA   Ciordia S., Albar J.P., Alcaide M., La Cono V., Yakimov M.M., Antunes A.,
RA   Taborda M., Da Costa M.S., Amann R.I., Gloeckner F.O., Golyshina O.V.,
RA   Golyshin P.N., Teeling H.;
RT   "Halorhabdus tiamatea: proteogenomics and glycosidase activity measurements
RT   identify the first cultivated euryarchaeon from a deep-sea anoxic brine
RT   lake as potential polysaccharide degrader.";
RL   Environ. Microbiol. 16:2525-2537(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; HF571520; CCQ33926.1; -; Genomic_DNA.
DR   EMBL; AFNT02000026; ERJ05750.1; -; Genomic_DNA.
DR   RefSeq; WP_008523688.1; NZ_AFNT02000026.1.
DR   STRING; 1033806.HTIA_1802; -.
DR   GeneID; 23799633; -.
DR   KEGG; hti:HTIA_1802; -.
DR   PATRIC; fig|1033806.12.peg.1789; -.
DR   eggNOG; arCOG02233; Archaea.
DR   HOGENOM; CLU_008878_4_1_2; -.
DR   OrthoDB; 346033at2157; -.
DR   Proteomes; UP000003861; Unassembled WGS sequence.
DR   Proteomes; UP000015381; Chromosome.
DR   GO; GO:0047833; F:D-sorbitol dehydrogenase (acceptor) activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   InterPro; IPR022357; MIP_CS.
DR   PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR   PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
DR   PROSITE; PS00221; MIP; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000313|EMBL:ERJ05750.1}.
FT   DOMAIN          204..234
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   553 AA;  59471 MW;  F1AD97B9819565C1 CRC64;
     MSGGRRSNDR ADRTPIEDAD VCIVGAGPAG ALIAHRLAAV GHEVVVLEAG PRFDPEARIE
     QMEDALRPAH GRPDVWGMGG ERDAYTSSGD RHYPLNHTRV KGVGGSTLHW QGMVMRLHER
     DFAVASQDGV AADWPIEYDD LRPYYAEAET ALGIAGASDN PFEPPREQPH PMAAFEPSHS
     DSIFAEACEA LGITTHSVPN ARNSEPYDDR SACVGYGTCQ PVCPSGAKYD ATSHVEKAEA
     AGARVVDRVP VQRLEHDDAG EAVTAAVYAT PDGETYRQEA REFVLAAGGV ETPRLLLLSD
     SPQYPDGLAN SSGLVGRYFH EHLFAGTSGV IDRETRQHHV GFNTTESHQF YDEPAAGTGQ
     GIPAAEADAD DLGPIKLEFR NYGGPSPVGL ALSDGGWGEA LRERVADAYG NHLTVGALVE
     QTPRRENRVA LDPSITDDHG NPVPEIHWDL DDRTRRTLRR ANAIQEGILE ELDAEITWQI
     GPENTGPAFH HMGTTRMGAD PEESVVDGRG RTHDLANLWL AGSSVFPTGG AMNPTLSIAA
     LALRAADHVA EKL
//
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