ID C5AZT4_METEA Unreviewed; 373 AA.
AC C5AZT4;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 98.
DE SubName: Full=Alcohol dehydrogenase, zinc-binding, Isopropanol dehydrogenase (IPDH-like) {ECO:0000313|EMBL:ACS41458.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:ACS41458.1};
GN Name=adh {ECO:0000313|EMBL:ACS41458.1};
GN OrderedLocusNames=MexAM1_META1p3748 {ECO:0000313|EMBL:ACS41458.1};
OS Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS 9133 / AM1) (Methylobacterium extorquens).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=272630 {ECO:0000313|EMBL:ACS41458.1, ECO:0000313|Proteomes:UP000009081};
RN [1] {ECO:0000313|EMBL:ACS41458.1, ECO:0000313|Proteomes:UP000009081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
RC {ECO:0000313|Proteomes:UP000009081};
RX PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA Lidstrom M.E.;
RT "Methylobacterium genome sequences: a reference blueprint to investigate
RT microbial metabolism of C1 compounds from natural and industrial sources.";
RL PLoS ONE 4:E5584-E5584(2009).
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|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; CP001510; ACS41458.1; -; Genomic_DNA.
DR RefSeq; WP_012753348.1; NC_012808.1.
DR AlphaFoldDB; C5AZT4; -.
DR STRING; 272630.MexAM1_META1p3748; -.
DR KEGG; mea:Mex_1p3748; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_3_5; -.
DR OMA; PTSYECG; -.
DR OrthoDB; 9773078at2; -.
DR Proteomes; UP000009081; Chromosome.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08285; NADP_ADH; 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; IPR020843; PKS_ER.
DR PANTHER; PTHR42813:SF4; DEHYDROGENASE 1, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 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 ECO:0000313|EMBL:ACS41458.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009081};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 29..371
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 373 AA; 39627 MW; ADEB99FF3AC384BB CRC64;
MNGQAETRIT ERNRARAARM KAAIFVEPGR IVLDEKPVPE VGPLDALIRI TTTTICGTDI
HILKGEYPVA RGLTIGHEPV GIIERLGSAV RGFQEGQRVV AGAITPSGHS AACLCGCLSQ
DGPDTKYGFK PMGGWRFGNT IDGSQAEYLL VPDAMTNLAP VPDDLSDEQV LMCPDIMSTG
FSGAESGGVR IGDTVAVFAQ GPIGLCATAG ARLMGATRII AVECVPERQQ VARSMGADEI
VDFSKEDPVD AILRITDGRG VDVAIEALGR QSTFEAALRV LRPGGTLASL GVYSEDLRIP
LGPFVAGLGN HTIVTTLCPG GKERMRRLMS VVASGRIDAR ALVTHRFRLE AIEEAYDLFA
HQRDGVLKVA ITP
//