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Database: UniProt
Entry: A0A068RZS2_9FUNG
LinkDB: A0A068RZS2_9FUNG
Original site: A0A068RZS2_9FUNG 
ID   A0A068RZS2_9FUNG        Unreviewed;       325 AA.
AC   A0A068RZS2;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Mannitol {ECO:0000313|EMBL:CDH55499.1};
GN   ORFNames=LCOR_06637.1 {ECO:0000313|EMBL:CDH55499.1};
OS   Lichtheimia corymbifera JMRC:FSU:9682.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX   NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH55499.1, ECO:0000313|Proteomes:UP000027586};
RN   [1] {ECO:0000313|EMBL:CDH55499.1, ECO:0000313|Proteomes:UP000027586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA   Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA   Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA   Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA   Voigt K.;
RT   "Gene expansion shapes genome architecture in the human pathogen
RT   Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT   terrestrial Mucorales (Mucoromycotina).";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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:CDH55499.1}.
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DR   EMBL; CBTN010000030; CDH55499.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068RZS2; -.
DR   VEuPathDB; FungiDB:LCOR_06637.1; -.
DR   OrthoDB; 5353053at2759; -.
DR   Proteomes; UP000027586; Unassembled WGS sequence.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   CDD; cd05283; CAD1; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR047109; CAD-like.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000027586};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..325
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001652782"
FT   DOMAIN          13..117
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          158..281
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   325 AA;  34820 MW;  779B57DDACA7ABB5 CRC64;
     MLTKWKYSFL LVACSCGTDI HQLTDGWGRA TFPLVPGHEF IGPVTAVGDA VTELKVGDRV
     GVSPVSRSCG TCVECTSSHG QLCPTRVPTY CGVYKGSPTY GGYANKVRLQ ASWAVKIPEN
     IPDEEGAPLL CAGITTFAPF KHENINENSS VGVVGIGGLG HLALQWARAK NCKRVIAVSS
     SKAKAAEATE LGATDFIALQ DGIPSEYLKS VDYLLVCGSG KSTDWNQLIT LIKNHGKLIL
     MDVPEQPLSI SPTLLVYSHI SIVGTFVGSN DDLKEMLALA SEKGVRPWIQ RVGNSLDEVN
     RGIQTVLDGK ARYRVVICGQ GRESN
//
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