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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//