ID A0A0C2G406_9ACTN Unreviewed; 494 AA.
AC A0A0C2G406;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:KIH97998.1};
GN ORFNames=LP52_15880 {ECO:0000313|EMBL:KIH97998.1};
OS Streptomonospora alba.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Streptomonospora.
OX NCBI_TaxID=183763 {ECO:0000313|EMBL:KIH97998.1, ECO:0000313|Proteomes:UP000031675};
RN [1] {ECO:0000313|Proteomes:UP000031675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 90003 {ECO:0000313|Proteomes:UP000031675};
RX PubMed=25601074; DOI=10.1016/j.chembiol.2014.11.017;
RA Metelev M., Tietz J.I., Melby J.O., Blair P.M., Zhu L., Livnat I.,
RA Severinov K., Mitchell D.A.;
RT "Structure, bioactivity, and resistance mechanism of streptomonomicin, an
RT unusual lasso Peptide from an understudied halophilic actinomycete.";
RL Chem. Biol. 22:241-250(2015).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986}.
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:KIH97998.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JROO01000030; KIH97998.1; -; Genomic_DNA.
DR RefSeq; WP_040274552.1; NZ_JROO01000030.1.
DR AlphaFoldDB; A0A0C2G406; -.
DR STRING; 183763.LP52_15880; -.
DR OrthoDB; 3802174at2; -.
DR Proteomes; UP000031675; Unassembled WGS sequence.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR PANTHER; PTHR42986; BENZALDEHYDE DEHYDROGENASE YFMT; 1.
DR PANTHER; PTHR42986:SF1; BENZALDEHYDE DEHYDROGENASE YFMT; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000031675}.
FT DOMAIN 22..480
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 52674 MW; 5A7C0992BCEE33EE CRC64;
MPAGQLPDPY TVSDRMPLGG AWRPGSSGTT ATDVNPYDDR PVAEFGLADA GDVERSFGAA
QEAQRSWADT PAPERAELFL RAMAVMDARK DEIVDWLVAE TGGIRERAEF EWGLVRAGMA
EVVSYPARVS GRILPGTVPG KENRVYRQPL GVVSVISPWN FPMQLSHRSL APALALGNAV
VLKPAGDTPV TGGTLLARIY EEAGLPPGLL SVVIGKSSEI GDPLVTHETS RLISFTGSTP
VGESIAAKAP LKRRALELGG NGPLVVLDDA DVERAVEAAL FGSYYHQGQI CMATNRVIVD
DAVHDDFVDR LTERVRGLRV GDPSDPQTQI GPVVNDSQRD DILDKISRAV DDGAELVLSG
EPTGPAGRVI PPHLVLGGND VATAAEEVFG PVSTVVRARG EEHALQLADA TEYGLSSAVY
TGDAERGVRF AQRVEAGMTH VNDTTVNDEP NTAFGGEKAS GIGRFGGEWA IEEFTRDHWV
SVQHTYRNLP FSSG
//