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Database: UniProt
Entry: Q5KVH3_GEOKA
LinkDB: Q5KVH3_GEOKA
Original site: Q5KVH3_GEOKA 
ID   Q5KVH3_GEOKA            Unreviewed;       503 AA.
AC   Q5KVH3;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   24-JAN-2024, entry version 104.
DE   SubName: Full=5-carboxy-2-hydroxymuconate semialdehyde dehydrogenase {ECO:0000313|EMBL:BAD77313.1};
GN   OrderedLocusNames=GK3028 {ECO:0000313|EMBL:BAD77313.1};
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909 {ECO:0000313|EMBL:BAD77313.1, ECO:0000313|Proteomes:UP000001172};
RN   [1] {ECO:0000313|EMBL:BAD77313.1, ECO:0000313|Proteomes:UP000001172}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426 {ECO:0000313|EMBL:BAD77313.1,
RC   ECO:0000313|Proteomes:UP000001172};
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(2004).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; BA000043; BAD77313.1; -; Genomic_DNA.
DR   RefSeq; WP_011232498.1; NC_006510.1.
DR   AlphaFoldDB; Q5KVH3; -.
DR   STRING; 235909.GK3028; -.
DR   KEGG; gka:GK3028; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_2_9; -.
DR   OMA; EGGHYSF; -.
DR   Proteomes; UP000001172; Chromosome.
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:UP000001172}.
FT   DOMAIN          16..477
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        253
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   503 AA;  55192 MW;  840B49DACA91DB83 CRC64;
     MAVQPKVLHY INGQFVEGAA GAYFDNINPF TNGTINQIAE GRKEDIDAAV RAAKEAFDHG
     PWRTMPVERR LRYLFRIADL IEQYADDIAY LEALDTGIPI SQAKKQAARA AENFRFYAEM
     VKTRLVGEAY HVNGQFLNYT VYKPVGVAGL ITPWNTPFML ETWKVAPALA TGNTVVLKPA
     EWSPLTANKL AEIIDEAGLP RGVFNVVHGF GETAGAALVA HPDVRLISFT GETTTGMEII
     RNSAATLKKT SMELGGKSPL IVFADADLER ALDAAVWGVF SLNGERCTAN SRLLLEQSIY
     DEFVARLKER VDRIVIGDPM APATELGPLI HRAHWERVNR YIDIAKQEGA DVYAPSVPTG
     LEKGNFVPPT LLLGCHNGMR VAQEEIFGPV MAVMSFADEE EAIRLANDVK YGLAAYVWTN
     DMKRGHRVAQ AIESGMAWVN SPNVRDLRIP FGGTKYSGIG REGGHYSFDF YTEVQVVHVA
     VGDPPIPSFG KAKPPSALSA EQK
//
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