ID A0A1D8A974_9SPHN Unreviewed; 471 AA.
AC A0A1D8A974;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:AOR78625.1};
GN ORFNames=BES08_10690 {ECO:0000313|EMBL:AOR78625.1};
OS Novosphingobium resinovorum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=158500 {ECO:0000313|EMBL:AOR78625.1, ECO:0000313|Proteomes:UP000094626};
RN [1] {ECO:0000313|Proteomes:UP000094626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA1 {ECO:0000313|Proteomes:UP000094626};
RX PubMed=27851894; DOI=10.1016/j.jbiotec.2016.11.013;
RA Hegedus B., Kos P.B., Balint B., Maroti G., Gan H.M., Perei K., Rakhely G.;
RT "Complete genome sequence of Novosphingobium resinovorum SA1, a versatile
RT xenobiotic-degrading bacterium capable of utilizing sulfanilic acid.";
RL J. Biotechnol. 241:76-80(2017).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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DR EMBL; CP017075; AOR78625.1; -; Genomic_DNA.
DR RefSeq; WP_069709219.1; NZ_CP017075.1.
DR AlphaFoldDB; A0A1D8A974; -.
DR KEGG; nre:BES08_10690; -.
DR OrthoDB; 9802947at2; -.
DR Proteomes; UP000094626; Chromosome.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd07138; ALDH_CddD_SSP0762; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR PANTHER; PTHR42804; ALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR42804:SF1; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345}.
FT DOMAIN 13..467
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 471 AA; 50319 MW; F41228AAFBB442C9 CRC64;
MRSYTQFYID GRWTSPVTPK TAEVINPATE EVSGEISLGS PADVDLAVAA ARRAFATYGE
SSVKDRLDLL ESIQAEYVRR EAELGEAIMV EMGAPKGLAN GFHTLLGKGH LGTAIEVLKE
FKFEEQRGVT LIRKEPIGVC GLITPWNWPM NQTCVKIFPA LAAGCTMILK PPQLAPYSAQ
ILAEILDKAG VPAGVFNMIQ GQGSVIGAAL TRHEDVDMIS FTGSEPVGVQ IQKDAADTVK
RVGLELGGKS AWIVLDDASL AANVAGATAG MMGNSGQTCS AGSRLLVPAS RLDDVKRAAA
EAANGVTVGD PQSDVAMGPV VSKSQYNIIQ QYIEKGLEEG AELIAGGLGR PEGLDKGWYV
KPTVFVGTND MVIAREEIFG PVLVIIPYDD IDDAVRIAND SNFGLGGYVS GEDLDTCRAV
SRRMRTGAIW VNGGFDFHAP FGGYKRSGNG REWGEFGFHE YLEVKSVIGW N
//
