ID Q1Q828_PSYCK Unreviewed; 333 AA.
AC Q1Q828;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 105.
DE SubName: Full=Alcohol dehydrogenase GroES-like protein {ECO:0000313|EMBL:ABE76175.1};
GN OrderedLocusNames=Pcryo_2398 {ECO:0000313|EMBL:ABE76175.1};
OS Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378
OS / K5).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=335284 {ECO:0000313|EMBL:ABE76175.1, ECO:0000313|Proteomes:UP000002425};
RN [1] {ECO:0000313|Proteomes:UP000002425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5
RC {ECO:0000313|Proteomes:UP000002425};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Richardson P.;
RT "Complete sequence of chromosome of Psychrobacter cryohalolentis K5.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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DR EMBL; CP000323; ABE76175.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1Q828; -.
DR STRING; 335284.Pcryo_2398; -.
DR KEGG; pcr:Pcryo_2398; -.
DR eggNOG; COG1064; Bacteria.
DR HOGENOM; CLU_026673_20_2_6; -.
DR OMA; FARNEHK; -.
DR Proteomes; UP000002425; Chromosome.
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 CDD; cd05283; CAD1; 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; IPR047109; CAD-like.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR PANTHER; PTHR42683:SF38; ALDEHYDE REDUCTASE AHR; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 11..330
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 333 AA; 36253 MW; 2D9AF8D051A04E8D CRC64;
MINAYAAKEK GGEFVPYQYD PGTLGDHEVE IEVHSCGICH SDLSMWQNEW GMTQYPFVGG
HEVAGKVLAK GKHVKHLELG DKVGLGWHKG YCNVCDLCIG GDHNLCPEQE GTIIGNHGGF
ADKVRAKDTS VIKIPEGLDF NAVGPLLCGG VTVFNPLMQY DITPTSRVAV IGIGGLGHLA
LQFANAWGCE VTAFTSESKM EEAKEMGAHH SLNSREDSEI EKAAGSFDLI ISTVNVDMNW
DVVIKTLRPK GKLHFVGLLE APLEISAAPM IMAQNSLSGS PVGSPSTLRK MLDFAARHNI
QPVTETYKMS EINEAFERLE SGNARYRVVL ERD
//