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Database: UniProt
Entry: D3D4I5_9ACTN
LinkDB: D3D4I5_9ACTN
Original site: D3D4I5_9ACTN 
ID   D3D4I5_9ACTN            Unreviewed;       507 AA.
AC   D3D4I5;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   SubName: Full=Aldehyde dehydrogenase (NAD(+)) {ECO:0000313|EMBL:EFC82179.1};
DE            EC=1.2.1.3 {ECO:0000313|EMBL:EFC82179.1};
GN   ORFNames=FrEUN1fDRAFT_4707 {ECO:0000313|EMBL:EFC82179.1};
OS   Parafrankia sp. EUN1f.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC   Parafrankia.
OX   NCBI_TaxID=102897 {ECO:0000313|EMBL:EFC82179.1, ECO:0000313|Proteomes:UP000004777};
RN   [1] {ECO:0000313|EMBL:EFC82179.1, ECO:0000313|Proteomes:UP000004777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EUN1f {ECO:0000313|EMBL:EFC82179.1,
RC   ECO:0000313|Proteomes:UP000004777};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Tice H., Bruce D., Goodwin L.,
RA   Pitluck S., Larimer F., Land M.L., Hauser L., Beauchemin N., Sen A.,
RA   Fernandez M., Tisa L.;
RT   "The draft genome of Frankia sp. EUN1f.";
RL   Submitted (JAN-2010) 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:EFC82179.1}.
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DR   EMBL; ADGX01000081; EFC82179.1; -; Genomic_DNA.
DR   RefSeq; WP_006542568.1; NZ_ADGX01000081.1.
DR   AlphaFoldDB; D3D4I5; -.
DR   Proteomes; UP000004777; Unassembled WGS sequence.
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; 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}.
FT   DOMAIN          35..494
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        263
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   507 AA;  55064 MW;  382BCE162F5D03F5 CRC64;
     MTIYARPGEP GSPVRYASRY DNIIGGEYVP PVKGRYFENP SPVTGQAFTE IARSSAEDVE
     KALDAAHAAA PAWGKTSVAA RADILNKIAD RMEANLELLA VGETWDNGKP VRETLAADIP
     LAVDHFRYFA GAIRAQEGTL SQLDEDTVAY HFREPLGVVG QIIPWNFPLL MATWKLAPAL
     AAGNAVVLKP AEQTPASINL LWELIGDLLP PGVLNVVQGF GVEAGKPLAS SPRIAKIAFT
     GETTTGRLIM QYASQNLIPV TLELGGKSPN IFFKDVLAEH DDFQDKCLEG FTMFALNQGE
     VCTCPSRALI DRSIFDDFLD AAAVRTKAVR QGNPLDTETM IGAQASSDQL EKILSYIDIG
     KKEGARLVLG GERAELGGDL SGGYYVQPTI FQGTNRMRIF QEEIFGPVVS VTSFDGYDDA
     IAQANDSLYG LGAGVWTRNG NLAYRAGRDI QAGRVWTNCY HLYPAHAAFG GYKQSGIGRE
     NHSMMLDHYQ QTKNLLVSYS PKAMGFF
//
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