ID D2ZZU6_NEIMU Unreviewed; 871 AA.
AC D2ZZU6;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN ORFNames=NEIMUCOT_06180 {ECO:0000313|EMBL:EFC87376.1};
OS Neisseria mucosa ATCC 25996.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=546266 {ECO:0000313|EMBL:EFC87376.1, ECO:0000313|Proteomes:UP000003344};
RN [1] {ECO:0000313|EMBL:EFC87376.1, ECO:0000313|Proteomes:UP000003344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25996 {ECO:0000313|EMBL:EFC87376.1,
RC ECO:0000313|Proteomes:UP000003344};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2009) 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:EFC87376.1}.
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DR EMBL; ACDX02000021; EFC87376.1; -; Genomic_DNA.
DR RefSeq; WP_003744378.1; NZ_ACDX02000021.1.
DR AlphaFoldDB; D2ZZU6; -.
DR STRING; 546266.NEIMUCOT_06180; -.
DR GeneID; 61323535; -.
DR eggNOG; COG1012; Bacteria.
DR eggNOG; COG1454; Bacteria.
DR Proteomes; UP000003344; 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:UP000003344}.
FT DOMAIN 13..275
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 469..856
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 871 AA; 94787 MW; 2D5F73183F18F1CA CRC64;
MNASADNVVS PAVAEVNSLV EKGLRSLDEF RKLNQEQIDY IVAKASIAAL DKHGVLAMHA
VEETGRGVFE DKATKNLFAC ENVVRRLRDL KTVGVISEDD VTGITEIADP VGVVCGIVPT
TNPTSTTIFK SLIALKTRNP IIFSFHPSAQ QCSAHAAQIV RDAAIAAGAP ENCIQWIEKP
SMEGTSALMK HPGVATILAT GGNAMVEAAY SCGKPALGVG AGNVPAYVEK TANIQQAAHD
IVMSKAFDNG MICASEQAVI ADKEIYKELV EEFKSYGVYF ANKKEKAMLE DFIFGVTANC
ANCGGAKLNS AVVGKPAAWI AEQAGFKVPE KTNIIIAECR EVGPNEPLTR EKLSPVLAML
KADSTEQGLQ FAEQMVAFDG LGHSAAIHTA DQELAKTFGT RVKALRVIWN SPSTFGGIGD
VYNAFLPSLT LGCGSYGKNS VGGNVSAVNL LNIKKVGRRR NNMQWFKVPA KIYFERDSIQ
YLQDMKDCEK VMIVTDRSMV DLGFVDKVTH QLHQRKNKVT IQLFTDVEAD PSVQTVYKGT
DLMRSFQPDT IIALGGGSPM DAAKAMWLFY EQPQVDFEDL VQKFMDIRKR AFRFPELGRK
AKFIGIPTTS GTGSEVTPFT VISDGDKKYP IADYSLTPTI AIVDPAFTMT VPAGVTADTG
LDVLTHAVEA YVSVLANDFT DGLALQAIKL VFQYLERSYK HGASDPEARE HMHNASTIAG
MAFSNAFLGI NHSMAHKIGG KYHVPHGRAN AILLPHVIRY NGTRPQKTAT WPKYNYYKAD
LKYQEIARTL GLPCATPAEG VESFARACHE LAVNVGIKMS FKEQGIDEKT FIDGRKELAM
LSFEDQCTPA NPRLALVADM EEILTKAYYG E
//
