ID E7GDX4_9FIRM Unreviewed; 889 AA.
AC E7GDX4;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN ORFNames=HMPREF9488_02967 {ECO:0000313|EMBL:EFW03777.1};
OS Coprobacillus cateniformis.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Coprobacillus.
OX NCBI_TaxID=100884 {ECO:0000313|EMBL:EFW03777.1, ECO:0000313|Proteomes:UP000003157};
RN [1] {ECO:0000313|EMBL:EFW03777.1, ECO:0000313|Proteomes:UP000003157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=29_1 {ECO:0000313|EMBL:EFW03777.1,
RC ECO:0000313|Proteomes:UP000003157};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Sibley C.D.,
RA White A., Strauss J., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., White J.,
RA Yandava C., Nusbaum C., Birren B.;
RT "The Genome Sequence of Coprobacillus sp. strain 29_1.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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}.
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:EFW03777.1}.
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DR EMBL; ADKX01000043; EFW03777.1; -; Genomic_DNA.
DR RefSeq; WP_008790054.1; NZ_WSNW01000001.1.
DR AlphaFoldDB; E7GDX4; -.
DR STRING; 100884.GCA_000269565_02579; -.
DR GeneID; 78230393; -.
DR eggNOG; COG1012; Bacteria.
DR eggNOG; COG1454; Bacteria.
DR HOGENOM; CLU_007207_1_0_9; -.
DR OrthoDB; 9804734at2; -.
DR Proteomes; UP000003157; Unassembled WGS sequence.
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.
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:UP000003157}.
FT DOMAIN 19..418
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 475..867
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 889 AA; 97674 MW; 190E369176F8151F CRC64;
MAEKKAVKKV EEPTNEQIDQ HVDELVQKAL VALDKFESFD QDAVDYIVAK CSVAGLDQHG
VLAEAAVKET GRGVFEDKAV KNLFACEYVT SNLRHLKTVG IINEDPLTGV TEIAEPVGVI
CGIVPTTNPT STVIFKSLIS LKTRNPIIFS FHPSAYECSV QAAKVVRDAA IAAGAPEDCI
QWLGLRSMYA TTALMNHPGV ATILATGGNA MVKAAYSCGK PALGVGAGNV PAYVEKSCVL
KRAVNDIVLS KSFDNGMICA SEQAAIVDQE IYKEFKEEIT RFKVHFVNAD EKAKLEAFMF
GCTSYTDKVN EAKLNPNVVG KDATWIAEQA GFKVPEDTQI ICAECKEVGP NEPLTREKLS
PVLAVLKATS TEDGIAKSAA MVEFNGLGHS AAIHTQNHDI SVEFGLKCKA IRVIENAPST
FGGIGSVYNA FIPSLTLGCG SYGHNSVSNN VSAVNLLNIK RIGRRNNNMQ WVKLPPKIYF
ERNSIRYLRD MKVMEKAMIV TDRGMYNLGY VDKIEDVIKR RRNKVDMELY FDVEPDPSID
TVNEGVEIMR KFQPDVIIAL GGGSSMDAAK VMWLMYEHPE VNFDDIKQKF MDIRKRAFKF
PELGKKARLI CIPTTSGTGS EVTPFAVITD KQANKKYPLT DYSLTPTVAI IDPEFVMSLP
ASIAADTGID VLTHAVEAYV SILASDFTDG WAKQAVKLVF DYLELSVKEG NNHPEAREKM
HNAATIAGMA FANAFLGMNH SLAHKIGGEW HVPHGRTNGI LLPHVIRYNG TIPTKLNIWP
KIENYKADIK YMELAQLIGL KPKTPAEGVA MFADACEELC AKVGVACNIK SQGIDKAAWE
ESVHRMAMNA YEDQCTPANP RMPMVHDMEA ILRMIYDYES KFATETPKK
//
