ID F9F572_FUSOF Unreviewed; 392 AA.
AC F9F572;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Alcohol dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FOXB_01547 {ECO:0000313|EMBL:EGU87956.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU87956.1};
RN [1] {ECO:0000313|EMBL:EGU87956.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU87956.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {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:EGU87956.1}.
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DR EMBL; AFQF01000493; EGU87956.1; -; Genomic_DNA.
DR AlphaFoldDB; F9F572; -.
DR STRING; 660025.F9F572; -.
DR PaxDb; 5507-FOXG_11415P0; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08282; PFDH_like; 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 PANTHER; PTHR42813:SF3; GLUTATHIONE-INDEPENDENT FORMALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 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 Metal-binding {ECO:0000256|RuleBase:RU361277};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 44..147
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 196..268
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 392 AA; 42200 MW; 5721C8EC34A9C4A2 CRC64;
MTTQTMKAVN YQGPYKVKVQ EIELPKLEHP DDVIVKVSQW LINAQAAICG SDLHMYEGRT
AAEPGITFGH ENMGIVEQLG EGVTLLKKGD RVVMPFNVAD GRCRNCEEGR TAFCTGVNPG
FAGGAYGYVA MGPYRGGQAQ YIRVPYADFN ALKLPAGKEH EADFILLADI FPTGWHGVEI
SGFRSGESVA VFGAGPVGLM AAYSAVLRGA SRVFVVDRVP ERLQAAEKIG CTPIDFSKGD
AVDMIIKAND GEEVDRSVDA VGYQAVSKSG DTEQPNIVLE NMIKVTRACG GLGIPGLYVP
SDPGASDEAS AKGMISLSFG KLFEKGLTIG TGQCNVKSYN RYLRDLIISG RAKPSFVVSH
EINIEEAEVA YEKFDKRIDG YTKVLIHPNG GF
//
