ID G7ZH28_AZOL4 Unreviewed; 506 AA.
AC G7ZH28;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:CBS90689.1};
DE EC=1.2.1.3 {ECO:0000313|EMBL:CBS90689.1};
GN Name=aldB {ECO:0000313|EMBL:CBS90689.1};
GN OrderedLocusNames=AZOLI_p40300 {ECO:0000313|EMBL:CBS90689.1};
OS Azospirillum lipoferum (strain 4B).
OG Plasmid AZO_p4 {ECO:0000313|EMBL:CBS90689.1,
OG ECO:0000313|Proteomes:UP000005667}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS90689.1, ECO:0000313|Proteomes:UP000005667};
RN [1] {ECO:0000313|Proteomes:UP000005667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RC PLASMID=Plasmid AZO_p4 {ECO:0000313|Proteomes:UP000005667};
RX PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA Zhulin I.B.;
RT "Azospirillum genomes reveal transition of bacteria from aquatic to
RT terrestrial environments.";
RL PLoS Genet. 7:E1002430-E1002430(2011).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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DR EMBL; FQ311872; CBS90689.1; -; Genomic_DNA.
DR RefSeq; WP_014189541.1; NC_016587.1.
DR AlphaFoldDB; G7ZH28; -.
DR KEGG; ali:AZOLI_p40300; -.
DR HOGENOM; CLU_005391_0_2_5; -.
DR OrthoDB; 9772584at2; -.
DR Proteomes; UP000005667; Plasmid AZO_p4.
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 CDD; cd07559; ALDH_ACDHII_AcoD-like; 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 PANTHER; PTHR43111; ALDEHYDE DEHYDROGENASE B-RELATED; 1.
DR PANTHER; PTHR43111:SF1; ALDEHYDE DEHYDROGENASE B-RELATED; 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}; Plasmid {ECO:0000313|EMBL:CBS90689.1}.
FT DOMAIN 27..492
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 506 AA; 55532 MW; 3B2197F519358D0F CRC64;
MLHQALDTLQ KQIALRPRYD NYIGGQWVAP VDGQYFTNLT PITGKPLCEV ARSQAADIEL
ALDAAHAART AWGRTSPTER SNILLKIADR MEERLEVIAL AETLDNGKPI RETRAADVPL
AIDHFRYYAG CIRAQEGSIG EIDHHTYAYH FHEPLGVVGQ IIPWNFPLLM AAWKLAPALA
AGNCIVLKPA EQTPMAIMVL AEIIGDLLPP GVLNIVNGFG LEAGKPLATN KRIAKIAFTG
ETSTGRLILQ YAAENIIPST VELGGKSPNI FFEDVMAEDD DFLDKALEGF AMFALNQGEV
CTCPSRVLIQ KSIYDRFIKL AVERVAKIAQ GHPLDGGTMI GAQASQEQLE KILSYIEIGK
AEGAKVLLGG ERAHLGGELE GGYYVQPTIL EGHNKMRIFQ EEIFGPVVAV TTFETEEEAL
AIANDSEFGL GAGVWTRDGS RYFRMGRAIQ AGRVWTNCYH LYPAHAAFGG YKKSGIGRET
HKMMLDHYQQ TKCLLVSYSP KALGFF
//
