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Database: UniProt
Entry: A0A0L0V3J8_9BASI
LinkDB: A0A0L0V3J8_9BASI
Original site: A0A0L0V3J8_9BASI 
ID   A0A0L0V3J8_9BASI        Unreviewed;       398 AA.
AC   A0A0L0V3J8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=L-arabinitol 4-dehydrogenase {ECO:0000256|ARBA:ARBA00039783};
DE            EC=1.1.1.12 {ECO:0000256|ARBA:ARBA00038954};
GN   ORFNames=PSTG_12770 {ECO:0000313|EMBL:KNE93857.1};
OS   Puccinia striiformis f. sp. tritici PST-78.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=1165861 {ECO:0000313|EMBL:KNE93857.1, ECO:0000313|Proteomes:UP000054564};
RN   [1] {ECO:0000313|Proteomes:UP000054564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race PST-78 {ECO:0000313|Proteomes:UP000054564};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Hulbert S., Chen X., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Puccinia striiformis f. sp. tritici PST-78.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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         ECO:0000256|RuleBase:RU361277};
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, ECO:0000256|RuleBase:RU361277}.
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:KNE93857.1}.
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DR   EMBL; AJIL01000128; KNE93857.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L0V3J8; -.
DR   STRING; 1165861.A0A0L0V3J8; -.
DR   OrthoDB; 3017546at2759; -.
DR   Proteomes; UP000054564; 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   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0019568; P:arabinose catabolic process; IEA:UniProtKB-KW.
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; IPR002328; ADH_Zn_CS.
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.
DR   PROSITE; PS00059; ADH_ZINC; 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   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054564};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          72..185
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          226..357
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   398 AA;  43141 MW;  5559AFC17017030B CRC64;
     MCGPTFKPDP VFQSINPALY DPRNVLDSAE FEILTDANKV KAYSDENKNI ACCYNDKQQI
     LMVNKPIPKA HPGQVLLHIR ATGICGSDVH FWKHSRVGEK MVVKHECGAG HESAGEVIGL
     GEGVTHLKIG DRVAVEAGVP CSKPTCEQCR KGCYNACPQM IFFSTPPYHG LLTRFHAHPA
     CWVHKIPDHV SYEEGSLLEP LAVALAGIER AGVRLGDPVL ICGAGPIGLV TLLACHAAGA
     CPIAITDLST ARLDFAKRLL PSVTTIQIER GTLERDVAEQ VKEAMGCNPR VALECTGFES
     SIAGAIYSVS FGGKVFVIGV GGDKFTLPFS HMSENEIDLQ FQFRYANQYP KAIRLVSSGL
     IDLKPLVTHR FPLHKAVEAF HTSADITSGS IKVQIIDF
//
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