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Database: UniProt
Entry: A0A0M2LLJ6_9MICO
LinkDB: A0A0M2LLJ6_9MICO
Original site: A0A0M2LLJ6_9MICO 
ID   A0A0M2LLJ6_9MICO        Unreviewed;       498 AA.
AC   A0A0M2LLJ6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Betaine-aldehyde dehydrogenase {ECO:0000313|EMBL:KKI16629.1};
DE            EC=1.2.1.8 {ECO:0000313|EMBL:KKI16629.1};
GN   ORFNames=XM48_14450 {ECO:0000313|EMBL:KKI16629.1};
OS   Leucobacter sp. Ag1.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leucobacter.
OX   NCBI_TaxID=1642040 {ECO:0000313|EMBL:KKI16629.1, ECO:0000313|Proteomes:UP000033836};
RN   [1] {ECO:0000313|EMBL:KKI16629.1, ECO:0000313|Proteomes:UP000033836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ag1 {ECO:0000313|EMBL:KKI16629.1,
RC   ECO:0000313|Proteomes:UP000033836};
RA   Pei D., Kukutla P., Yu W., Xu J.;
RT   "Draft Genome Sequences of Leucobacter sp. Ag1 from Mosquito Anopheles
RT   gambiae.";
RL   Submitted (APR-2015) 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:KKI16629.1}.
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DR   EMBL; LAYO01000109; KKI16629.1; -; Genomic_DNA.
DR   RefSeq; WP_046456543.1; NZ_LAYO01000109.1.
DR   AlphaFoldDB; A0A0M2LLJ6; -.
DR   STRING; 1642040.XM48_14450; -.
DR   PATRIC; fig|1642040.3.peg.628; -.
DR   OrthoDB; 6882680at2; -.
DR   Proteomes; UP000033836; Unassembled WGS sequence.
DR   GO; GO:0018480; F:5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC.
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:UP000033836}.
FT   DOMAIN          21..481
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        258
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   498 AA;  53789 MW;  FFCEA731A8EF1B6D CRC64;
     MTHQKPEGLP EKIQLFIDGE FVDAQDGATF DVIEPVSNEV YITAASAGKA DVDRAVAAAK
     RAFDEGPWPK MLPRERSRIL HRVADIVESR DEQLALLESW DSGLPITQAK GQARRAAENF
     RFFADLIVAE HDNVTKVPGR QINYVNRKPK GVAGLITPWN VPFMQESWKL APAIATGNTV
     VLKPASYTPL SAALWPEIFR EAGVPEGVFN LILGSGGVAG DALVKHPDVP LISFTGDSST
     GAMISTNAAP FLKGLSLELG GKSPSVVFAD ADLEEALDAT VFSVFSLNGE RCTAGSRVLV
     ERSIYDDFVA RYSERAKNIV IGLPSDPATE VGALVHPSHF EKVMSYVEIG KSEGRLVAGG
     GRPEGFPEGN YVAPTVFADV KPDARIFQEE IFGPVVAITP FDTDEEALEL ANDTKYGLAA
     YVWTSNLKRA HNFAHGIESG MVWLNSNNVR DLRTPFGGVK ASGLGREGGY RSVDFYTTAQ
     SIQITLNEAH SPRFGAGK
//
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