ID G9MIK2_HYPVG Unreviewed; 377 AA.
AC G9MIK2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=L-arabinitol 4-dehydrogenase {ECO:0000256|ARBA:ARBA00039783};
DE EC=1.1.1.12 {ECO:0000256|ARBA:ARBA00038954};
GN ORFNames=TRIVIDRAFT_54807 {ECO:0000313|EMBL:EHK25319.1};
OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK25319.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK25319.1, ECO:0000313|Proteomes:UP000007115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arabinitol + NAD(+) = H(+) + L-xylulose + NADH;
CC Xref=Rhea:RHEA:16381, ChEBI:CHEBI:15378, ChEBI:CHEBI:17399,
CC ChEBI:CHEBI:18403, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00035840};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC arabinitol; D-xylulose 5-phosphate from L-arabinose (fungal route):
CC step 2/5. {ECO:0000256|ARBA:ARBA00037881}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072}.
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:EHK25319.1}.
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DR EMBL; ABDF02000003; EHK25319.1; -; Genomic_DNA.
DR RefSeq; XP_013959528.1; XM_014104053.1.
DR AlphaFoldDB; G9MIK2; -.
DR STRING; 413071.G9MIK2; -.
DR EnsemblFungi; EHK25319; EHK25319; TRIVIDRAFT_54807.
DR GeneID; 25795464; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_54807; -.
DR eggNOG; KOG0024; Eukaryota.
DR HOGENOM; CLU_026673_11_5_1; -.
DR InParanoid; G9MIK2; -.
DR OMA; FILGHEC; -.
DR OrthoDB; 3017546at2759; -.
DR Proteomes; UP000007115; 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; cd05285; sorbitol_DH; 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; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR045306; SDH-like.
DR PANTHER; PTHR43161:SF12; L-ARABINITOL 4-DEHYDROGENASE; 1.
DR PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 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 3: Inferred from homology;
KW Arabinose catabolism {ECO:0000256|ARBA:ARBA00022935};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022935};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007115};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 53..164
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 203..335
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 377 AA; 39969 MW; DF0648981559DEF1 CRC64;
MSPSAVDDAP KARGAAISVK PNIGVFTNPK HDLWISEAEP SADAVKSGAE LKPGEVTIAV
RSTGICGSDV HFWHAGCIGP MIVEGDHILG HESAGEVIAV HPTVTSLQVG DRVAIEPNVI
CNACEPCLTG RYNGCEKVEF LSTPPVPGLL RRYVNHPAVW CHKIGNMSWE NGALLEPLSV
ALAGMQRAKV QLGDPVLVCG AGPIGLVSML CCAAAGACPL VITDISESRL AFAKEICPRV
VTHQIQIGKS AEETAKGIVG AFGGIEPAVT MECTGVESSI ASAIWATKFG GKVFVIGVGK
NEINIPFMRA SVREVDIQLQ YRYSNTWPRA IRLIESGVLD LSKFVTHRFP LEEAVKAFET
SADPKSGAIK VMIQSLD
//