ID C7ND57_LEPBD Unreviewed; 875 AA.
AC C7ND57;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN OrderedLocusNames=Lebu_2076 {ECO:0000313|EMBL:ACV39935.1};
OS Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / NCTC
OS 10249 / C-1013-b).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=523794 {ECO:0000313|EMBL:ACV39935.1, ECO:0000313|Proteomes:UP000001910};
RN [1] {ECO:0000313|EMBL:ACV39935.1, ECO:0000313|Proteomes:UP000001910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b
RC {ECO:0000313|Proteomes:UP000001910};
RX PubMed=21304648; DOI=10.4056/sigs.1854;
RA Ivanova N., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D.,
RA Goodwin L., Brettin T., Detter J.C., Han C., Pitluck S., Mikhailova N.,
RA Pati A., Mavrommatis K., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Chain P., Rohde C., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Leptotrichia buccalis type strain (C-1013-
RT b).";
RL Stand. Genomic Sci. 1:126-132(2009).
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; CP001685; ACV39935.1; -; Genomic_DNA.
DR RefSeq; WP_015770270.1; NC_013192.1.
DR AlphaFoldDB; C7ND57; -.
DR STRING; 523794.Lebu_2076; -.
DR KEGG; lba:Lebu_2076; -.
DR eggNOG; COG1012; Bacteria.
DR eggNOG; COG1454; Bacteria.
DR HOGENOM; CLU_007207_1_0_0; -.
DR OrthoDB; 9804734at2; -.
DR Proteomes; UP000001910; 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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000111}.
FT DOMAIN 8..268
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 455..848
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
FT COILED 3..30
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 875 AA; 96805 MW; 730BE6F8D6CC5A20 CRC64;
MAVVKDLESL KELIQRVRKA QEEFATFDQE RVDKIFRKVA QKMNDERITL ANLAVAETGM
GIVEDKVIKN HFASEYIYNK YKDEKTCGVL EDDRSYGVKK IATPIGIIAG IVPTTNPTST
AMFKTLISLK TRNAIIFSPH PRAKQATIET AKIALETAVK YGAPKDIIGW IDEPSVELSR
ELMASADLIL ATGGPGMVKA AYSSGTPAIG VGAGNTPVVI DKSADIKMTA NYILMSKTFD
NGVICATEQS VIIDKEIYDK VRSEFLNRGA YILNEEELNK VREILFINGN LNAEVVGKSA
YVIAGMAGFE IPKSSKVLIG EVESTATEEP FAHEKLSPVL AMYKSENFED SLKKADELVR
LGGLGHTSSL YINLAEKEKI DKFGRLMKTG RTLINMPASL GAIGDVFNFK LEPSLTLGCG
SWGGNSVSEN VGVKHLLNVK TIAERRENML WFKVPEKIYF KYGSLPTALE ELKGSHKKAF
IVTDKVLAEL GYAEHITKVL DEINIDYRIF SEVKEDPTLS SAQAGAKAML EYNPDVVIAL
GGGSAMDAAK IMWVLYEHPE LRFRDLAMRF MDIRKRIVEF PEMGKKAKFI AVATSAGTGS
EVTPFSVITD DETGIKYPLA DYALTPHVAI NDPELMLTMP KGLTIASGID VFTHALESYV
SIMATEYTKP YSKEAARLVF KYLPESVDLG AKAIKAKEKM ANASCLAGMA FANAFLGINH
SLAHKLGGKF HVPHGIANAM LLEEVIRFNA VEAPTKMGLF PQYRYPDAMQ RYAEMNDYLG
FGGNTKEEKV ENLIKGINEL NRRIGIPASI KEWGVPEKDF LEAVDEMSLD AFDDQCTPAN
PRYPLMEELR EIYLKSYYGK EWENEKERVA QILGF
//
