ID A0A083ZZP8_9GAMM Unreviewed; 890 AA.
AC A0A083ZZP8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN Name=adhE_2 {ECO:0000313|EMBL:KEY58527.1};
GN ORFNames=SRDD_27750 {ECO:0000313|EMBL:KEY58527.1};
OS Serratia sp. DD3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=1410619 {ECO:0000313|EMBL:KEY58527.1, ECO:0000313|Proteomes:UP000017810};
RN [1] {ECO:0000313|EMBL:KEY58527.1, ECO:0000313|Proteomes:UP000017810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD3 {ECO:0000313|EMBL:KEY58527.1,
RC ECO:0000313|Proteomes:UP000017810};
RX PubMed=25212623;
RA Poehlein A., Freese H.M., Daniel R., Simeonova D.D.;
RT "Draft Genome Sequence of Serratia sp. Strain DD3, Isolated from the Guts
RT of Daphnia magna.";
RL Genome Announc. 2:e00903-14(2014).
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:KEY58527.1}.
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DR EMBL; AYKS02000071; KEY58527.1; -; Genomic_DNA.
DR RefSeq; WP_023489995.1; NZ_AYKS02000071.1.
DR AlphaFoldDB; A0A083ZZP8; -.
DR STRING; 1410619.SRDD_27750; -.
DR eggNOG; COG1012; Bacteria.
DR eggNOG; COG1454; Bacteria.
DR OrthoDB; 9815791at2; -.
DR Proteomes; UP000017810; 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.
DR PROSITE; PS00060; ADH_IRON_2; 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:UP000017810}.
FT DOMAIN 5..280
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 890 AA; 96240 MW; E3605978F1FA51C6 CRC64;
MAVTNVAELN ELVARVKKAQ REYANYSQEQ VDNIFRAAAL AAADARIPLA KMAVEESGMG
IIEDKVIKNH FASEYIYNAY KDEKTCGILS EDDTFGTITI AEPIGLLCGI VPTTNPTSTA
IFKALISLKT RNGIIFSPHP RAKNATNKAA DIVLQAAIAA GAPKDIIGWI DQPTVDLSNQ
LMHHPDINLI LATGGPGMVK AAYSSGKPAI GVGAGNTPVV IDETADIKRA VASILMSKTF
DNGVICASEQ SVIVVDSAYD AVRERFASHG GYMLQGKELK AVQDIILKNG GLNAAIVGQS
APKIAEMAGI QVPANTKILI GEVKVVDETE PFAHEKLSPT LAMYRAKDFA DAVSKAEKLV
AMGGIGHTSC LYTDQDNQTE RVEFFGDKMK TARILVNTPA SQGGIGDLYN FKLAPSLTLG
CGSWGGNSIS ENVGPKHLIN KKTVAKRAEN MLWHKLPKSI YFRRGSLPIA LEEVASDGAK
RAFIVTDRYL FNNGYADQIT KVLKSHGIET EVFFEVEADP TLSIVRKGAE QMNSFKPDVI
IALGGGSPMD AAKIMWVLYE HPETHFEDLA LRFMDIRKRI YKFPKMGVKA KMIAVTTTSG
TGSEVTPFAV VTDDATGQKY PLADYALTPD MAIVDANLVM NMPKSLCAYG GLDAVTHALE
AYVSVLANEY SDGQALQALK LLKEYLPASY RDGAKNPVAR ERVHNAATIA GIAFANAFLG
VCHSMAHKLG SEFHIPHGLA NAMLIANVIR YNANDNPTKQ TAFSQYDRPQ ARRRYAEIAD
HLGLSAAGDR TAQKIEKLLK WLDEIKTELG IPASIRDAGV PEVDFLAKVD KLSEDAFDDQ
CTGANPRYPL IAELKQILMD TYYGHAFSEA LEDTVVAAPV AAKAEKKSKK
//
