ID E1SP69_FERBD Unreviewed; 868 AA.
AC E1SP69;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN OrderedLocusNames=Fbal_1490 {ECO:0000313|EMBL:ADN75694.1};
OS Ferrimonas balearica (strain DSM 9799 / CCM 4581 / KCTC 23876 / PAT).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Ferrimonadaceae; Ferrimonas.
OX NCBI_TaxID=550540 {ECO:0000313|EMBL:ADN75694.1, ECO:0000313|Proteomes:UP000006683};
RN [1] {ECO:0000313|EMBL:ADN75694.1, ECO:0000313|Proteomes:UP000006683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9799 / CCM 4581 / KCTC 23876 / PAT
RC {ECO:0000313|Proteomes:UP000006683};
RX DOI=10.4056/sigs.1161239;
RA Nolan M., Sikorski J., Davenport K., Lucas S., Glavina Del Rio T., Tice H.,
RA Cheng J., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y., Jeffries C., Tapia R., Brettin T., Detter J., Han C.,
RA Yasawong M., Rohde M., Tindall B., Goker M., Woyke T., Bristow J.,
RA Eisen J., Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Lapidus A.;
RT "Complete genome sequence of Ferrimonas balearica type strain (PAT).";
RL Stand. Genomic Sci. 3:174-182(2010).
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SIMILARITY: In the C-terminal section; belongs to the iron-containing
CC alcohol dehydrogenase family. {ECO:0000256|ARBA:ARBA00035645,
CC ECO:0000256|PIRNR:PIRNR000111}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the aldehyde
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00035641,
CC ECO:0000256|PIRNR:PIRNR000111}.
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DR EMBL; CP002209; ADN75694.1; -; Genomic_DNA.
DR RefSeq; WP_013345000.1; NC_014541.1.
DR AlphaFoldDB; E1SP69; -.
DR STRING; 550540.Fbal_1490; -.
DR GeneID; 67181708; -.
DR KEGG; fbl:Fbal_1490; -.
DR eggNOG; COG1012; Bacteria.
DR eggNOG; COG1454; Bacteria.
DR HOGENOM; CLU_007207_1_1_6; -.
DR OrthoDB; 9815791at2; -.
DR Proteomes; UP000006683; Chromosome.
DR GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006066; P:alcohol metabolic process; IEA:InterPro.
DR GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR CDD; cd08178; AAD_C; 1.
DR CDD; cd07122; ALDH_F20_ACDH; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR034789; AAD_C.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR012079; Bifunc_Ald-ADH.
DR PANTHER; PTHR11496; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR11496:SF83; HYDROXYACID-OXOACID TRANSHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF00171; Aldedh; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PIRSF; PIRSF000111; ALDH_ADH; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
DR PROSITE; PS00060; ADH_IRON_2; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000111};
KW Reference proteome {ECO:0000313|Proteomes:UP000006683}.
FT DOMAIN 4..266
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 455..843
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 868 AA; 93284 MW; C5E1B37894DF25A1 CRC64;
MSEHTELDAL VARVKAAQEA FASYSQEQVD AIFRAASLAA ADARIPLAMM AAEETGMGVA
EDKVIKNHFA SEYIYNKYRD EKTCGVLSED EAFGTMTIAE PVGIVCGIVP TTNPTSTAIF
KALICLKTRN GIIFSPHPRA KRSTCEAARI VLEAAVKAGA PKDIVGWVAE PSVAASNALM
RHDDIALILA TGGPGMVKAA YSSGKPAIGV GAGNTPVVID DSADIKQAVA SIQLSKTFDN
GVICASEQAV VVVDSVYDQV RERFASTGSY VLSAEECERL KSVILNDGHL NADIVGQPAW
KIAGMADITV PKSTKILIGE VSSTGLEEPF AHEKLSPVLG LYRASDFEDA VVKAEALVAL
GGIGHTSVLY CDQDLQKERV LTFGQRMKTA RILINTPASQ GGIGDLYNFK LAPSLTLGCG
SWGGNSISEN VGPKHLINTK TVAKRAENML WHRLPEKIYF RRGALPIALE ELKGKSRALI
VTDHYLFNNG YCDRVLEILK GMGLETEVFF EVEADPTLAI VRKGAALCQS FQPDVLIALG
GGSPMDAAKI MWVLYEYPET QFHDLALRFM DIRKRIFQFP KLGQKAEFVA IPTTSGTGSE
VTPFAVVTDD STGQKYPLAD YELTPNMAIV DPDLVMNMPA SLTAFGGIDA VTHALEAYVS
VLANEYSDGQ ALQALKLLFA HLPESYHKGA AAPKAKEKVH NAATIAGIAF ANAFLGICHS
MAHKLGSEFH LAHGLANALL ISNVIRYNAT DVPTKQAAFS QYDRPTALCR YGEIADHLGL
GGSDNAEKVE RLVAAIDALK AELDIPESIQ AAGVPEAEFL ARLDELAIEA FDDQCTGANP
RFPLISELKQ LLLDSYYGRP YRENGDNA
//
