ID S3MX39_9GAMM Unreviewed; 387 AA.
AC S3MX39;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:EPF70998.1};
GN ORFNames=F945_02761 {ECO:0000313|EMBL:EPF70998.1};
OS Acinetobacter rudis CIP 110305.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=421052 {ECO:0000313|EMBL:EPF70998.1, ECO:0000313|Proteomes:UP000014568};
RN [1] {ECO:0000313|EMBL:EPF70998.1, ECO:0000313|Proteomes:UP000014568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 110305 {ECO:0000313|EMBL:EPF70998.1,
RC ECO:0000313|Proteomes:UP000014568};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter rudis CIP 110305.";
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007358}.
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:EPF70998.1}.
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DR EMBL; ATGI01000034; EPF70998.1; -; Genomic_DNA.
DR RefSeq; WP_016657146.1; NZ_KE340354.1.
DR AlphaFoldDB; S3MX39; -.
DR STRING; 632955.GCA_000829675_01870; -.
DR PATRIC; fig|421052.3.peg.2696; -.
DR eggNOG; COG1454; Bacteria.
DR HOGENOM; CLU_007207_0_0_6; -.
DR OrthoDB; 9815791at2; -.
DR Proteomes; UP000014568; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd08194; Fe-ADH-like; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR PANTHER; PTHR11496; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR11496:SF102; ALCOHOL DEHYDROGENASE 4; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000014568}.
FT DOMAIN 8..376
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 387 AA; 41254 MW; 29C415E6769E2733 CRC64;
MSHAIQLPRM MEVGKNARAK LPQILAALGC HKPLIITDKI MVSLGYIQQI QTLLLEANIQ
ADYFDQTIPE PTSASITAGV THIRTHQYDA IIAVGGGSPI DSAKAMSILA KFGGEIRDYK
FPRQVNEAGL PIIAIPTTAG TGSECTRFTI ITDDVSSEKM LCAGIGFLPV AAIVDYELTM
SLPARTTADT GIDALTHAIE AYVSAKANAY SDAQALAAMS LIGPNLQTVY HEPDNEQARE
QMMLGSTLAG IAFSNASVAL VHGMSRPIGA FFHVPHGLSN AMLLPSVTAY SIPAAPTRYA
TCAKAIGVAH ADDSDEIANE KLIQALIKIN QDLNVPTLAE FGVDKAEFDQ VLHTMAEQAL
ASGSPNNNPR VPSIAEMKQL YQALWNS
//
