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ADH2_ZYMMO
ID   ADH2_ZYMMO              Reviewed;         383 AA.
AC   P0DJA2; P06758; Q5NM40;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Alcohol dehydrogenase 2;
DE            EC=1.1.1.1;
DE   AltName: Full=Alcohol dehydrogenase II;
DE            Short=ADH II;
GN   Name=adhB; OrderedLocusNames=ZMO1596;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=3584063; DOI=10.1128/jb.169.6.2591-2597.1987;
RA   Conway T., Sewell G.W., Osman Y.A., Ingram L.O.;
RT   "Cloning and sequencing of the alcohol dehydrogenase II gene from Zymomonas
RT   mobilis.";
RL   J. Bacteriol. 169:2591-2597(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-50.
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=2935393; DOI=10.1111/j.1432-1033.1986.tb09366.x;
RA   Neale A.D., Scopes R.K., Kelly J.M., Wettenhall R.E.H.;
RT   "The two alcohol dehydrogenases of Zymomonas mobilis. Purification by
RT   differential dye ligand chromatography, molecular characterisation and
RT   physiological roles.";
RL   Eur. J. Biochem. 154:119-124(1986).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC         Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC         Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC         ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- MISCELLANEOUS: In Z.mobilis there are two isozymes of alcohol
CC       dehydrogenase.
CC   -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; M15394; AAA27683.1; -; Genomic_DNA.
DR   EMBL; AE008692; AAV90220.1; -; Genomic_DNA.
DR   PIR; A25978; A25978.
DR   RefSeq; WP_000168720.1; NZ_CP035711.1.
DR   PDB; 3OWO; X-ray; 2.07 A; A/B/C/D=1-383.
DR   PDB; 3OX4; X-ray; 2.00 A; A/B/C/D=1-383.
DR   PDBsum; 3OWO; -.
DR   PDBsum; 3OX4; -.
DR   AlphaFoldDB; P0DJA2; -.
DR   SMR; P0DJA2; -.
DR   STRING; 264203.ZMO1596; -.
DR   EnsemblBacteria; AAV90220; AAV90220; ZMO1596.
DR   GeneID; 58027316; -.
DR   KEGG; zmo:ZMO1596; -.
DR   eggNOG; COG1454; Bacteria.
DR   HOGENOM; CLU_007207_0_0_5; -.
DR   OMA; LPHTAHY; -.
DR   OrthoDB; 1456634at2; -.
DR   BioCyc; MetaCyc:MON-16805; -.
DR   BRENDA; 1.1.1.1; 14380.
DR   EvolutionaryTrace; P0DJA2; -.
DR   Proteomes; UP000001173; Chromosome.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   InterPro; IPR001670; ADH_Fe/GldA.
DR   InterPro; IPR018211; ADH_Fe_CS.
DR   InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR   PANTHER; PTHR11496; PTHR11496; 1.
DR   Pfam; PF00465; Fe-ADH; 1.
DR   PROSITE; PS00913; ADH_IRON_1; 1.
DR   PROSITE; PS00060; ADH_IRON_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Iron; NAD; Oxidoreductase;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2935393"
FT   CHAIN           2..383
FT                   /note="Alcohol dehydrogenase 2"
FT                   /id="PRO_0000087815"
FT   CONFLICT        38
FT                   /note="S -> G (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        45..48
FT                   /note="SGVV -> GVS (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          4..7
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   STRAND          10..15
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   HELIX           18..24
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   TURN            25..28
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   STRAND          33..39
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   HELIX           40..44
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   HELIX           47..56
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   TURN            57..59
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   STRAND          61..68
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   HELIX           74..86
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   STRAND          90..97
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   HELIX           98..112
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   HELIX           117..120
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   STRAND          122..124
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   STRAND          133..137
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   STRAND          139..141
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   TURN            144..146
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   STRAND          148..154
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   TURN            155..158
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   STRAND          159..164
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   HELIX           166..168
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   STRAND          171..175
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   HELIX           177..179
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   TURN            180..182
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   HELIX           185..204
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   HELIX           210..232
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   HELIX           237..257
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   HELIX           261..272
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   HELIX           277..306
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   HELIX           316..333
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   STRAND          338..340
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   TURN            341..344
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   HELIX           347..349
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   HELIX           350..357
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   HELIX           361..365
FT                   /evidence="ECO:0007829|PDB:3OX4"
FT   HELIX           372..381
FT                   /evidence="ECO:0007829|PDB:3OX4"
SQ   SEQUENCE   383 AA;  40145 MW;  E1C3A159B1652342 CRC64;
     MASSTFYIPF VNEMGEGSLE KAIKDLNGSG FKNALIVSDA FMNKSGVVKQ VADLLKAQGI
     NSAVYDGVMP NPTVTAVLEG LKILKDNNSD FVISLGGGSP HDCAKAIALV ATNGGEVKDY
     EGIDKSKKPA LPLMSINTTA GTASEMTRFC IITDEVRHVK MAIVDRHVTP MVSVNDPLLM
     VGMPKGLTAA TGMDALTHAF EAYSSTAATP ITDACALKAA SMIAKNLKTA CDNGKDMPAR
     EAMAYAQFLA GMAFNNASLG YVHAMAHQLG GYYNLPHGVC NAVLLPHVLA YNASVVAGRL
     KDVGVAMGLD IANLGDKEGA EATIQAVRDL AASIGIPANL TELGAKKEDV PLLADHALKD
     ACALTNPRQG DQKEVEELFL SAF
 
 
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