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Database: UniProt
Entry: A0A0P8WW37_9CLOT
LinkDB: A0A0P8WW37_9CLOT
Original site: A0A0P8WW37_9CLOT 
ID   A0A0P8WW37_9CLOT        Unreviewed;       456 AA.
AC   A0A0P8WW37;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN   Name=mdlD {ECO:0000313|EMBL:KPU42463.1};
GN   ORFNames=OXPF_42480 {ECO:0000313|EMBL:KPU42463.1};
OS   Oxobacter pfennigii.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Oxobacter.
OX   NCBI_TaxID=36849 {ECO:0000313|EMBL:KPU42463.1, ECO:0000313|Proteomes:UP000050326};
RN   [1] {ECO:0000313|EMBL:KPU42463.1, ECO:0000313|Proteomes:UP000050326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3222 {ECO:0000313|EMBL:KPU42463.1,
RC   ECO:0000313|Proteomes:UP000050326};
RA   Poehlein A., Bengelsdorf F.R., Schiel-Bengelsdorf B., Duerre P., Daniel R.;
RT   "Genome sequence of Oxobacter pfennigii DSM 3222.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492,
CC       ECO:0000256|RuleBase:RU003345}.
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:KPU42463.1}.
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DR   EMBL; LKET01000068; KPU42463.1; -; Genomic_DNA.
DR   RefSeq; WP_054877170.1; NZ_LKET01000068.1.
DR   AlphaFoldDB; A0A0P8WW37; -.
DR   STRING; 36849.OXPF_42480; -.
DR   PATRIC; fig|36849.3.peg.4487; -.
DR   OrthoDB; 9762913at2; -.
DR   Proteomes; UP000050326; Unassembled WGS sequence.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR   CDD; cd07136; ALDH_YwdH-P39616; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR   PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43570:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR036492};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050326}.
FT   DOMAIN          3..428
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        210
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ   SEQUENCE   456 AA;  51405 MW;  4984110ECA63EA5A CRC64;
     MYDVKKTIEK QRDFFDTGKT KDVSFRIAKL NLLRDTIKKY EGDIIAALKF DLNKAPFEAY
     ETEVGIVLEE IRYTIKHISN WARPKRIKTP VIHFLSSSYI YREPYGSVLI MSPWNYPFQL
     AVVPLIGAIA AGNCSIVKPS EYSFRTSEII EKIISEIFDE SFVAVVRGGR EANKRLLDEK
     FDYIFFTGSP QAGKIVMESA SKHLTPVTLE LGGKSPCIVD ETANVKLAAK RIVWGKFLNA
     GQTCVAPDYL LVHRSVKDEL ISEMKNCIKV FYGNNPAAND DYPKIINQKH FERLSGLMKS
     GRVVTGGQSN EKTRQIAPTI LEGITWESDV MQEEIFGPLL PIMEFEDLND ALDMVNRHPK
     PLAFYFFTTS KKNEVHAIRR ASFGGGCIND TIIHLSNSNL PFGGVGESGM GQYHGKGSYD
     TFTHKKSIIK KSNLLDVPLR YPPFRNHLGL LKKIMG
//
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