GenomeNet

Database: UniProt
Entry: A0A2N7QV98_9GAMM
LinkDB: A0A2N7QV98_9GAMM
Original site: A0A2N7QV98_9GAMM 
ID   A0A2N7QV98_9GAMM        Unreviewed;       507 AA.
AC   A0A2N7QV98;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=2-aminomuconic 6-semialdehyde dehydrogenase {ECO:0000313|EMBL:PMQ05576.1};
DE            EC=1.2.1.32 {ECO:0000313|EMBL:PMQ05576.1};
GN   Name=amnC {ECO:0000313|EMBL:PMQ05576.1};
GN   ORFNames=DyAD56_09605 {ECO:0000313|EMBL:PMQ05576.1};
OS   Dyella sp. AD56.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dyella.
OX   NCBI_TaxID=1528744 {ECO:0000313|EMBL:PMQ05576.1, ECO:0000313|Proteomes:UP000235676};
RN   [1] {ECO:0000313|EMBL:PMQ05576.1, ECO:0000313|Proteomes:UP000235676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD56 {ECO:0000313|EMBL:PMQ05576.1,
RC   ECO:0000313|Proteomes:UP000235676};
RA   Schulz-Bohm K., Janssens T.K., De Jager V., Gawehns F., De Boer W.,
RA   Garbeva P.;
RT   "Bacterial performance in fungal presence.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
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:PMQ05576.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; NRDP01000011; PMQ05576.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N7QV98; -.
DR   Proteomes; UP000235676; Unassembled WGS sequence.
DR   GO; GO:0047102; F:aminomuconate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   CDD; cd07093; ALDH_F8_HMSADH; 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   PANTHER; PTHR43720; 2-AMINOMUCONIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43720:SF2; 2-AMINOMUCONIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR   Pfam; PF00171; Aldedh; 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|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235676}.
FT   DOMAIN          45..503
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        274
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   507 AA;  54652 MW;  6A5FD01C3D45BC88 CRC64;
     MRIVTRRIRS RPVQLKTPGL KLAQMPTLRL ANLIDGRLQA PRNDRWLDVF EPATGQVFAH
     CPDSTSDDVA DAVAAARRAA PGWAATPTEQ RASLLYRLAD LVEARTDEFV ALESRDSGKP
     LVQARNLDIP RAVSNLRFFA AAIMGWSSES HAMEIGAINY TLRQPLGVVG CISPWNLPLY
     LFTWKIAPAL AAGNTVVSKP SEITPCTAAL LGELSIEACF PPGVFNIVQG RGPSVGQAIV
     EHAAVKAVSF TGSTRTGAQI AAVAAPQFKK VSLELGGKNP AIVFEDADLS DTNLDTIVRS
     GFANQGEICL CGSRLLVQRS IHETFRERYL ARVKALRVGD PNENNSDLGA LVSREHFDKV
     MGCIATAREE GGRILCGGKA ITVDGRCASG WFVAPTVIDG LGSDTATNQH EIFGPVVSLI
     PFEDEAEALA IANGTGYGLA ASVWTRDLSR AHRFGAQLDF GIVWTNCWLL RDLRTPFGGT
     KQSGLGREGG AEALRFFTEP KNICIRY
//
DBGET integrated database retrieval system