ID A0A140NGM5_PROSM Unreviewed; 886 AA.
AC A0A140NGM5;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000256|PIRNR:PIRNR000111};
GN OrderedLocusNames=S70_00650 {ECO:0000313|EMBL:AFH92031.1};
OS Providencia stuartii (strain MRSN 2154).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=1157951 {ECO:0000313|EMBL:AFH92031.1, ECO:0000313|Proteomes:UP000005012};
RN [1] {ECO:0000313|EMBL:AFH92031.1, ECO:0000313|Proteomes:UP000005012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSN 2154 {ECO:0000313|EMBL:AFH92031.1,
RC ECO:0000313|Proteomes:UP000005012};
RX PubMed=22740665; DOI=10.1128/JB.00615-12;
RA Clifford R.J., Hang J., Riley M.C., Onmus-Leone F., Kuschner R.A.,
RA Lesho E.P., Waterman P.E.;
RT "Complete Genome Sequence of Providencia stuartii Clinical Isolate MRSN
RT 2154.";
RL J. Bacteriol. 194:3736-3737(2012).
RN [2] {ECO:0000313|Proteomes:UP000005012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSN 2154 {ECO:0000313|Proteomes:UP000005012};
RA Clifford R.J., Hang J., Riley M.C., Onmus-Leone F., Kuschner R.A.,
RA Lesho E.P., Waterman P.E.;
RT "Complete genome sequence of Providencia stuartii clinical isolate MRSN
RT 2154.";
RL Submitted (APR-2012) 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}.
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DR EMBL; CP003488; AFH92031.1; -; Genomic_DNA.
DR RefSeq; WP_014656066.1; NC_017731.1.
DR AlphaFoldDB; A0A140NGM5; -.
DR GeneID; 79053823; -.
DR KEGG; psi:S70_00650; -.
DR PATRIC; fig|1157951.4.peg.131; -.
DR HOGENOM; CLU_007207_2_0_6; -.
DR OrthoDB; 9815791at2; -.
DR Proteomes; UP000005012; 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.
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}.
FT DOMAIN 6..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 886 AA; 96305 MW; AE63CC25AEABBC7A CRC64;
MSVTNVTELN DLVARVKKAQ REFANFSQEQ VDRIFRAAAL AAADARIPLA KLAVEESGMG
IVEDKVIKNH FASEYIYNAY KDEKTCGVLS EDPTFGTITI AEPIGIICGI VPTTNPTSTA
IFKSLISLKT RNAIIFSPHP RAKNATNKAA EIVLKAAIEA GAPKDIIGWI DAPSVELSNA
LMHHEDINLI LATGGPGMVK AAYSSGKPAI GVGAGNTPVV IDETADIKRA VASILMSKTF
DNGVICASEQ SVVVVDEIYN QVRERFATHG GYILQGKELK AVQDVILKNG SLNAAIVGQT
AYKIAEMAGV TVPVTTKILI GEVKVIADSE PFAHEKLSPL LAMYRAKNFE EAVDKAEQLV
EMGGIGHTSC LYTDQDNQAE RVNYFGVKMK TARILINTPA SQGGIGDLYN FKLAPSLTLG
CGSWGGNSIS ENVGPKHLIN TKTVAKRAEN MLWHKLPNSI YFRRGCLPIA LEEIATDGAK
RAFIVTDGYL FNNGYVEEVV NVLKKHHIET DVFFEVEADP TLTVVRKGAA QMNAFKPDVI
IALGGGSPMD AAKIMWVMYE HPETHFEELA LRFMDIRKRI HRFPKMGVKA KLVAITTTSG
TGSEVTPFAV VTDDKTGQKY PLADYALTPN MAIVDANLVM NMPKSLTAFG GLDAVTHAME
AYVSVLANEY SDGQALQALS LLKEYLPTSY HEGATNPVAR ERVHNAATIA GIAFANAFLG
VCHSMAHKLG SEFHIPHGLA NALLISNVVR YNANDNPTKQ TAFSQYDRPQ ARRRYAEIAD
HLGLTKSSDR TDAKIEKLLA WLEEIKADLG IPKSIREAGV PEADFLARVD KLSEDAFDDQ
CTGANPRYPL ISELKQLLLD SYYGREFTEQ TSTTTAAKVE KKSSKK
//