ID A0A0R1H2M0_9LACO Unreviewed; 870 AA.
AC A0A0R1H2M0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN ORFNames=FC07_GL001093 {ECO:0000313|EMBL:KRK40233.1};
OS Loigolactobacillus bifermentans DSM 20003.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Loigolactobacillus.
OX NCBI_TaxID=1423726 {ECO:0000313|EMBL:KRK40233.1, ECO:0000313|Proteomes:UP000051461};
RN [1] {ECO:0000313|EMBL:KRK40233.1, ECO:0000313|Proteomes:UP000051461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20003 {ECO:0000313|EMBL:KRK40233.1,
RC ECO:0000313|Proteomes:UP000051461};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRK40233.1}.
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DR EMBL; AZDA01000018; KRK40233.1; -; Genomic_DNA.
DR RefSeq; WP_057903750.1; NZ_AZDA01000018.1.
DR AlphaFoldDB; A0A0R1H2M0; -.
DR STRING; 1423726.FC07_GL001093; -.
DR PATRIC; fig|1423726.3.peg.1132; -.
DR OrthoDB; 9815791at2; -.
DR Proteomes; UP000051461; 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:UP000051461}.
FT DOMAIN 19..276
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 465..850
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 870 AA; 95459 MW; 94309233FD49354F CRC64;
MSKEQITKPK EEVDVNGMID ELVKKSHVSL KEMATFTQEQ VDKVCEAVAL AALDNHMKIA
KMAVAETKRG VVEDKAIKNM YASEYIWNSI RDDKTVGIID DDDEKQMMKI AEPVGVVAGV
TPVTNPTSTV VFKTLISLKT RNTIIFGFHP QAQNCCVETA KIIRAAAIEA GAPEDAIQWI
SKPSIEATGA LMNHDGVATV LATGGPGMVK AAYSTGKPAL GVGPGNGPSY IEATADIKQA
VNDIVLSKTF DNGMVCASEN SAVVDASIYD KVKQEFEYWN CYFLKKSEVP ALEEAMFDAK
RGGVKGPIAG KSAYDIAKLA GINVAPDTKV LIAETDGVGP KYPISREKLS PVLSMYKANG
HEAAFKRCLE LLEFGGLGHT ASLHTRDEDL ITEFGLKMPA CRVLINQPSA VGGIGNIYNN
MVPSLTLGTG SYGKNSISHN VTDWDLLNIK TVAKRRNNMQ WVKLPPKVYF ERNSVRYLET
MEGINRAFLV CDPGMVQFGY SDRVLAELRK RKNNVEIEIF SQVEPNPSIE TVEKGVAQMD
AFKPDTIIAL GGGSAMDAGK FMWLMYEHPD VSFFGAKQKF LDIRKRTYKV PTSNKAKYIG
IPTTSGTGSE VTPYAVITDN KTHIKYPITD YAMQPDIAII DSQFVETVPP RTTAWTGLDA
ITHATEAYVS TMSTEYTRGW ALQALKLAFD NLKASYEGDK EARYNMANAS TMAGMSFASA
FLGINHSIAH KLGGEFNLPH GLAIAITYPH VVRYNATTPT KLAMWPRYNH FRALKDYADI
ARYLGFEGNT DEELKESLVK HFVDLAHSVD VTLSLKANRV EKAHFDATVD ELASLSYEDQ
CTTANPKEPL ISELKQILID EYDGKGVETK
//
