ID A5EU08_BRASB Unreviewed; 795 AA.
AC A5EU08;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 92.
DE SubName: Full=Putative membrane-anchored aldehyde dehydrogenase protein {ECO:0000313|EMBL:ABQ39652.1};
DE EC=1.2.1.3 {ECO:0000313|EMBL:ABQ39652.1};
GN OrderedLocusNames=BBta_7827 {ECO:0000313|EMBL:ABQ39652.1};
OS Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=288000 {ECO:0000313|EMBL:ABQ39652.1, ECO:0000313|Proteomes:UP000000246};
RN [1] {ECO:0000313|EMBL:ABQ39652.1, ECO:0000313|Proteomes:UP000000246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTAi1 / ATCC BAA-1182 {ECO:0000313|Proteomes:UP000000246};
RX PubMed=17540897; DOI=10.1126/science.1139548;
RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C.,
RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., Saunders E.,
RA Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL Science 316:1307-1312(2007).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|PIRNR:PIRNR036490, ECO:0000256|RuleBase:RU003345}.
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DR EMBL; CP000494; ABQ39652.1; -; Genomic_DNA.
DR RefSeq; WP_012047537.1; NC_009485.1.
DR AlphaFoldDB; A5EU08; -.
DR STRING; 288000.BBta_7827; -.
DR KEGG; bbt:BBta_7827; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_018339_0_0_5; -.
DR OMA; MDYGPAP; -.
DR OrthoDB; 9812625at2; -.
DR Proteomes; UP000000246; Chromosome.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
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; IPR011408; Aldehyde_DH.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR PANTHER; PTHR11699:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 2.
DR PIRSF; PIRSF036490; Aldedh_dupl; 1.
DR SUPFAM; SSF53720; ALDH-like; 2.
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 45..487
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 539..762
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 266
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 795 AA; 84999 MW; 06E656C965D2F076 CRC64;
MSIAHYFDTM DYGSAPEADG EARAWLKRHE ATFGHFIAGK FAAPASGKHL ATIEPATGKP
LARIAQGVAA DVEAAVGAAR AAQLPWAKLG GHGRARHLYA LARMLQRHAR LFAVLESIDN
GKPIRETRDL DVPLAARHFL YHAGWAQLQE REFADHVPVG VIGQIIPWNF PLLMLAWKIA
PALAAGNTVV LKPAEFTSLT ALLFAELAAD AGLPPGVLNV VTGDGATGAL LVDNPGVDKI
AFTGSTEVGR LIRQSTAGSG KSLTLELGGK SPFIVFEDAD LDGAVEGVVD AIWFNQGQVC
CAGSRLLLQE GIAETFRRRL IRRMETLRVG PPLDKTIDMG AVVAPVQLER IKALVETGVK
EGAEKYQASG AIPAEGCFYP PTLLWNVHPS STVAIEEIFG PVVVAMTFRT PDEAVMLANN
TRYGLAASVW SETIGLALDI APKLQAGVVW VNATNLFDAS VGFGGCRESG FGREGGREGI
YEYLKPKAWS GRTARAKLPP LPEASTEGAG FGTPSIDRTA KLFLGGKQVR PDGNYARAVL
SPKGKPLGEV GEGNRKDIRN AVAAARSAEA WARVTAHNRA QILYYLGENL SARSDEFARR
IGELTGVSPA KARAEVEASI ERLFSYGAWA DKYEGTIHTP PLRGVALAMH EPIGVVGVVC
PDEAPLLGFI SLVAPLIAMG NRVVAVPSER HPLAATDFYQ VLETSDVPAG VVNIVTGERD
ALAKVLAEHD DVDALWVFGS QEASTMAERL SVGNLKRTLV DHGLALDWYD RAASEGPILL
RHAVRVKNIW IPYGD
//