ID A0A0Q4MXI2_9GAMM Unreviewed; 892 AA.
AC A0A0Q4MXI2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN ORFNames=ASF13_16260 {ECO:0000313|EMBL:KQN53152.1};
OS Erwinia sp. Leaf53.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=1736225 {ECO:0000313|EMBL:KQN53152.1, ECO:0000313|Proteomes:UP000050856};
RN [1] {ECO:0000313|EMBL:KQN53152.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN53152.1,
RC ECO:0000313|Proteomes:UP000050856};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN53152.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN53152.1,
RC ECO:0000313|Proteomes:UP000050856};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQN53152.1}.
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DR EMBL; LMLK01000027; KQN53152.1; -; Genomic_DNA.
DR RefSeq; WP_056242162.1; NZ_LMLK01000027.1.
DR AlphaFoldDB; A0A0Q4MXI2; -.
DR STRING; 1736225.ASF13_16260; -.
DR Proteomes; UP000050856; 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:UP000050856}.
FT DOMAIN 5..399
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 457..849
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 892 AA; 96079 MW; 5BCF697EBADB924D CRC64;
MAVTNVAELN ALVARVKLAQ QQYASFTQSQ VDKIFRAAAL AAADARIPLA KLAVAESGMG
IVEDKVIKNH FASEYIYNAY KDEQTCGVLS TDDTFGTMII AEPVGLICGI VPTTNPTSTA
IFKALISLKT RNGIIFSPHP RAKDATNKAA EIVLRAAVAA GAPADIIGWI DAPTVDLSNQ
LMHHPDINLI LATGGPGMVK AAYSSGKPAI GVGAGNTPVV IDETADIKRA VASILMSKTF
DNGVICASEQ SVIVVASVYD AVRERFASHG GYLLQGEALK AVQAVILKNG ALNAAIVGQS
AEQIAALAGI SVPAGTKILI GEVQLIDESE PFAHEKLSPL LAMYRAKDFS DAVGKAEQLV
AMGGIGHTSC LYTDQDNQRE RVGLFGERMK TARILINTPA SQGGIGDLYN FKLAPSLTLG
CGSWGGNSIS ENVGPKHLIN RKTVAKRAEN MLWHKLPESI YFRRGSLPIA LDEVASDGAK
RAFIVTDRFL FNNGYTEQVT RVLKSHGVET DVFFEVEADP TLTTVRKGAE QMHAFKPDVI
IALGGGSPMD AAKIMWVMYE HPETHFEELA LRFMDIRKRI HKFPKMGVKA KMVAIATTSG
TGSEVTPFAV VTDDATGQKY PLADYALTPN MAIVDANLVM DMPKSLCAFG GIDAVTHSLE
AYVSVLANEF SDGQALQALK LLQENLPASY REGAKNPQAR ERVHNAATIA GIAFANAFLG
VCHSMAHKLG SEFHIPHGLS NALLLCNVIR YNANDNPTKQ TAFSQYDRPQ ARRRYAEVAD
HLNLSAPGDR TAQKIEKLLA WLDELKVQLD IPASIREAGV QEADFLAKVD QLAENAFDDQ
CTGANPRYPL IAELKQILLD SYYGRKFSEG VKPEEALADA ESNVKALKKA RR
//
