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Database: UniProt
Entry: A0A1J5LKD2_9PROT
LinkDB: A0A1J5LKD2_9PROT
Original site: A0A1J5LKD2_9PROT 
ID   A0A1J5LKD2_9PROT        Unreviewed;       503 AA.
AC   A0A1J5LKD2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase {ECO:0000313|EMBL:OIQ31411.1};
GN   ORFNames=BM562_07520 {ECO:0000313|EMBL:OIQ31411.1};
OS   Alphaproteobacteria bacterium MedPE-SWcel.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=1860092 {ECO:0000313|EMBL:OIQ31411.1, ECO:0000313|Proteomes:UP000183546};
RN   [1] {ECO:0000313|EMBL:OIQ31411.1, ECO:0000313|Proteomes:UP000183546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MedPE-SWcel {ECO:0000313|EMBL:OIQ31411.1};
RX   PubMed=27446036; DOI=10.3389/fmicb.2016.00996;
RA   Lopez-Perez M., Kimes N.E., Haro-Moreno J.M., Rodriguez-Valera F.;
RT   "Not All Particles Are Equal: The Selective Enrichment of Particle-
RT   Associated Bacteria from the Mediterranean Sea.";
RL   Front. Microbiol. 7:996-996(2016).
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:OIQ31411.1}.
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DR   EMBL; MPDC01000009; OIQ31411.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J5LKD2; -.
DR   STRING; 1860092.BM562_07520; -.
DR   Proteomes; UP000183546; Unassembled WGS sequence.
DR   GO; GO:0018480; F:5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase activity; IEA:InterPro.
DR   GO; GO:1901023; P:4-hydroxyphenylacetate catabolic process; IEA:InterPro.
DR   CDD; cd07093; ALDH_F8_HMSADH; 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   InterPro; IPR011985; DH_HpaE.
DR   NCBIfam; TIGR02299; HpaE; 1.
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; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345}.
FT   DOMAIN          36..489
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   503 AA;  54535 MW;  64B5E6172DD1E87B CRC64;
     MSDLASNLAK LAPLLDRHKV NGITNLIGGK SCPSATGRTF DTLSPVDESV ICAVARSEST
     DIDAAAKAAK EAFPAWRDTP AADRQAILHR IADAIVERAE DIALCECWDT GQALRFMSKA
     ALRGADNFRF FGDRALTARD GQMLPSPTLM NVTTRVPIGP VGIITPWNTP FMLSTWKIAP
     ALAAGCTIVH KPAEFSPLTA RLLAEIAHDA GLPAGVWNLV NGYGEEAGKA LTEHPDIKAI
     AFVGESRTGS MIMAQGAPTL KRAHFELGGK NPVVVFDDAD LDRALDAAIF MIYSLNGERC
     TSSSRLLIQE SVADRFEAKL IDRVKKIRVG HPLDPATEVG PLIHKVHFDK VTSYFDTALR
     EGATIAAGGP RHGDRGWFVT PTLFTDASND MAIAQEEIFG PVLTMIRFKD EEDALAKAND
     TPYGLTGYIW TNDITRAMRF SHQLEAGMIW VNSENVRHLP TPFGGVKASG IGRDGGDWSF
     DFYMEQKHIG FATGQHKIPR LGA
//
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