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Database: UniProt
Entry: F7VAF2_9PROT
LinkDB: F7VAF2_9PROT
Original site: F7VAF2_9PROT 
ID   F7VAF2_9PROT            Unreviewed;       504 AA.
AC   F7VAF2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:GAA07347.1};
GN   ORFNames=ATPR_0351 {ECO:0000313|EMBL:GAA07347.1};
OS   Acetobacter tropicalis NBRC 101654.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=749388 {ECO:0000313|EMBL:GAA07347.1, ECO:0000313|Proteomes:UP000004319};
RN   [1] {ECO:0000313|EMBL:GAA07347.1, ECO:0000313|Proteomes:UP000004319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101654 {ECO:0000313|EMBL:GAA07347.1,
RC   ECO:0000313|Proteomes:UP000004319};
RX   PubMed=21554859; DOI=10.1016/j.bbrc.2011.04.126;
RA   Matsutani M., Hirakawa H., Nishikura M., Soemphol W., Ali I.A.I.,
RA   Yakushi T., Matsushita K.;
RT   "Increased number of Arginine-based salt bridges contributes to the
RT   thermotolerance of thermotolerant acetic acid bacteria, Acetobacter
RT   tropicalis SKU1100.";
RL   Biochem. Biophys. Res. Commun. 409:120-124(2011).
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:GAA07347.1}.
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DR   EMBL; BABS01000006; GAA07347.1; -; Genomic_DNA.
DR   RefSeq; WP_006557361.1; NZ_BABS01000006.1.
DR   AlphaFoldDB; F7VAF2; -.
DR   Proteomes; UP000004319; 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          38..491
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   504 AA;  53850 MW;  D0974EF4DAC85D50 CRC64;
     MSTLEENARK ANEYITRIRE KGVLNRIGGK ECPAISGEVF ETLSPIDLKP LASVAKGDAR
     DIDQAAKAAK AAQPAWAALS GTKRREILHT IADAIEARAE EIAFLECLDT GQSLRFMSKA
     ALRGAENFRY FADKAPSARN GLSLPTGGQA NITTRNPVGP VGVITPWNTP FMLSTWKIAP
     ALAAGCTVVH KPAEFSPITA SVLVEIAEKA GLPPGVWNLV NGFGEDAGAE LTRHPDIKAI
     AFVGESGTGS LIMKQAADTL KRFHFELGGK NPIIVFADAD LERAADAALF MIYSLNGERC
     TSSSRLLVEA SIYDKFTATL AERVKTIKVG HPLDPATVVG PLIHPVHEKK VLEYIGIGKE
     EGATIAAGGG KADGPGGGCY VAPTLFTHAT NNMRIAQEEI FGPVLTAIPF KSEDEAVLLA
     NDTQYGLAAY LWTSDVTRSF RVSDKLEAGM IWVNSENVRH LDTPFGGVKA SGIGRDGGDW
     SFDFYMETKN VSFATGVHTI PKLA
//
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