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Database: UniProt
Entry: J0KHF7_9BURK
LinkDB: J0KHF7_9BURK
Original site: J0KHF7_9BURK 
ID   J0KHF7_9BURK            Unreviewed;       485 AA.
AC   J0KHF7;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase {ECO:0000313|EMBL:EJE53070.1};
GN   ORFNames=PMI14_02329 {ECO:0000313|EMBL:EJE53070.1};
OS   Acidovorax sp. CF316.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1144317 {ECO:0000313|EMBL:EJE53070.1, ECO:0000313|Proteomes:UP000004811};
RN   [1] {ECO:0000313|EMBL:EJE53070.1, ECO:0000313|Proteomes:UP000004811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF316 {ECO:0000313|EMBL:EJE53070.1,
RC   ECO:0000313|Proteomes:UP000004811};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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:EJE53070.1}.
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DR   EMBL; AKJX01000099; EJE53070.1; -; Genomic_DNA.
DR   RefSeq; WP_007853664.1; NZ_AKJX01000099.1.
DR   AlphaFoldDB; J0KHF7; -.
DR   PATRIC; fig|1144317.3.peg.2019; -.
DR   Proteomes; UP000004811; 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; 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; 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; 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:UP000004811}.
FT   DOMAIN          16..471
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        242
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   485 AA;  51774 MW;  FFDB9A601BE780BD CRC64;
     MRIDHLIEGK PVAGREYFET VNPATQEVLA EVASGGAAEV NAAVAAAKDA FPAWAGLPAP
     ERAKLIRKLG DLIAAEVPQI AATETRDTGQ VIAQTGKALI PRAADNFYYF AEMCTRVDGH
     TYPTPTHLNY TLFHPVGVCA LISPWNVPFM TSTWKVAPAL AFGNTAVLKM SELSPLTAAR
     LGQLALEAGI PAGVLNVVHG FGKEAGEPLC AHPDVRAISF TGSTATGNRI VQAAGLKKFS
     MELGGKSPFV VFDDADLDRA LDAAVFMIFS NNGERCTAGS RILVQKSIYA DFAEKFAARA
     RRITVGDPMD DRTIIGPMIS PAHLAKVRSY IELGPKEGAT LLCGGLGAPE LPAHLHKGNF
     VRPTVFADVN NRMQIAQDEI FGPVACLIPF ADEAEAIRLA NDTQYGLSSY VWTENIGRAH
     RVAAGIEAGM CFVNSQNVRD LRQPFGGTKG SGTGREGGSW SYEVFLEPKN VAVSLGSHHI
     PHWGV
//
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