ALDH_VIBHA
ID ALDH_VIBHA Reviewed; 510 AA.
AC Q56694;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=NADP-dependent fatty aldehyde dehydrogenase;
DE EC=1.2.1.4;
GN Name=aldH;
OS Vibrio harveyi (Beneckea harveyi).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=669;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP CHARACTERIZATION.
RC STRAIN=ATCC 33843 / NCIMB 1871 / 392 / MAV;
RX PubMed=8527447; DOI=10.1021/bi00051a022;
RA Vedadi M., Szittner R., Smillie L., Meighen E.;
RT "Involvement of cysteine 289 in the catalytic activity of an NADP(+)-
RT specific fatty aldehyde dehydrogenase from Vibrio harveyi.";
RL Biochemistry 34:16725-16732(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RC STRAIN=ATCC 33843 / NCIMB 1871 / 392 / MAV;
RX PubMed=10903148; DOI=10.1042/bj3490853;
RA Ahvazi B., Coulombe R., Delarge M., Vedadi M., Zhang L., Meighen E.,
RA Vrielink A.;
RT "Crystal structure of the NADP+-dependent aldehyde dehydrogenase from
RT Vibrio harveyi: structural implications for cofactor specificity and
RT affinity.";
RL Biochem. J. 349:853-861(2000).
CC -!- FUNCTION: Catalyzes the oxidation of long-chain aliphatic aldehydes to
CC acids. May be implicated in controlling luminescence as it catalyzes
CC the oxidation of the fatty aldehyde substrate for the light-emitting
CC reaction.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NADP(+) = a carboxylate + 2 H(+) + NADPH;
CC Xref=Rhea:RHEA:11888, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.4;
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; U39638; AAA89078.1; -; Genomic_DNA.
DR PDB; 1EYY; X-ray; 2.50 A; A/B/C/D=1-510.
DR PDB; 1EZ0; X-ray; 2.10 A; A/B/C/D=1-510.
DR PDBsum; 1EYY; -.
DR PDBsum; 1EZ0; -.
DR AlphaFoldDB; Q56694; -.
DR SMR; Q56694; -.
DR STRING; 669.AL538_01810; -.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR EvolutionaryTrace; Q56694; -.
DR GO; GO:0033721; F:aldehyde dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR CDD; cd07129; ALDH_KGSADH; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
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; IPR044151; ALDH_KGSADH.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NADP; Oxidoreductase.
FT CHAIN 1..510
FT /note="NADP-dependent fatty aldehyde dehydrogenase"
FT /id="PRO_0000056466"
FT ACT_SITE 253
FT ACT_SITE 289
FT BINDING 229..234
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:1EYY"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:1EZ0"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:1EZ0"
FT HELIX 29..48
FT /evidence="ECO:0007829|PDB:1EZ0"
FT HELIX 51..67
FT /evidence="ECO:0007829|PDB:1EZ0"
FT HELIX 69..80
FT /evidence="ECO:0007829|PDB:1EZ0"
FT HELIX 84..107
FT /evidence="ECO:0007829|PDB:1EZ0"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:1EZ0"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1EZ0"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1EZ0"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:1EZ0"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:1EZ0"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1EYY"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:1EZ0"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:1EZ0"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:1EZ0"
FT HELIX 178..195
FT /evidence="ECO:0007829|PDB:1EZ0"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:1EZ0"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:1EZ0"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:1EZ0"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:1EZ0"
FT HELIX 231..243
FT /evidence="ECO:0007829|PDB:1EZ0"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:1EZ0"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:1EZ0"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:1EZ0"
FT HELIX 264..269
FT /evidence="ECO:0007829|PDB:1EZ0"
FT HELIX 273..281
FT /evidence="ECO:0007829|PDB:1EZ0"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:1EZ0"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:1EZ0"
FT HELIX 301..316
FT /evidence="ECO:0007829|PDB:1EZ0"
FT HELIX 325..339
FT /evidence="ECO:0007829|PDB:1EZ0"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:1EZ0"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:1EZ0"
FT HELIX 365..370
FT /evidence="ECO:0007829|PDB:1EZ0"
FT HELIX 372..375
FT /evidence="ECO:0007829|PDB:1EZ0"
FT STRAND 380..390
FT /evidence="ECO:0007829|PDB:1EZ0"
FT HELIX 391..399
FT /evidence="ECO:0007829|PDB:1EZ0"
FT STRAND 404..410
FT /evidence="ECO:0007829|PDB:1EZ0"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:1EZ0"
FT HELIX 416..427
FT /evidence="ECO:0007829|PDB:1EZ0"
FT STRAND 430..437
FT /evidence="ECO:0007829|PDB:1EZ0"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:1EZ0"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:1EYY"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:1EZ0"
FT HELIX 467..473
FT /evidence="ECO:0007829|PDB:1EZ0"
FT STRAND 474..481
FT /evidence="ECO:0007829|PDB:1EZ0"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:1EZ0"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:1EZ0"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:1EZ0"
SQ SEQUENCE 510 AA; 54460 MW; E132F2406AA3F47A CRC64;
MNPQTDNVFY ATNAFTGEAL PLAFPVHTEV EVNQAATAAA KVARDFRRLN NSKRASLLRT
IASELEARSD DIIARAHLET ALPEVRLTGE IARTANQLRL FADVVNSGSY HQAILDTPNP
TRAPLPKPDI RRQQIALGPV AVFGASNFPL AFSAAGGDTA SALAAGCPVI VKGHTAHPGT
SQIVAECIEQ ALKQEQLPQA IFTLLQGNQR ALGQALVSHP EIKAVGFTGS VGGGRALFNL
AHERPEPIPF YGELGAINPT FIFPSAMRAK ADLADQFVAS MTMGCGQFCT KPGVVFALNT
PETQAFIETA QSLIRQQSPS TLLTPGIRDS YQSQVVSRGS DDGIDVTFSQ AESPCVASAL
FVTSSENWRK HPAWEEEIFG PQSLIVVCEN VADMLSLSEM LAGSLTATIH ATEEDYPQVS
QLIPRLEEIA GRLVFNGWPT GVEVGYAMVH GGPYPASTHS ASTSVGAEAI HRWLRPVAYQ
ALPESLLPDS LKAENPLEIA RAVDGKAAHS
