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Database: UniProt
Entry: M9R7Z0_9RHOB
LinkDB: M9R7Z0_9RHOB
Original site: M9R7Z0_9RHOB 
ID   M9R7Z0_9RHOB            Unreviewed;       796 AA.
AC   M9R7Z0;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:AGI66421.1};
DE            EC=1.2.1.3 {ECO:0000313|EMBL:AGI66421.1};
GN   ORFNames=OAN307_c06940 {ECO:0000313|EMBL:AGI66421.1};
OS   Octadecabacter antarcticus 307.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Octadecabacter.
OX   NCBI_TaxID=391626 {ECO:0000313|EMBL:AGI66421.1, ECO:0000313|Proteomes:UP000005307};
RN   [1] {ECO:0000313|EMBL:AGI66421.1, ECO:0000313|Proteomes:UP000005307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=307 {ECO:0000313|EMBL:AGI66421.1,
RC   ECO:0000313|Proteomes:UP000005307};
RX   PubMed=23671678;
RA   Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K.,
RA   Brinkhoff T., Simon M., Daniel R.;
RT   "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High Genome
RT   Plasticity and a New Type of Xanthorhodopsin.";
RL   PLoS ONE 8:E63422-E63422(2013).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|PIRNR:PIRNR036490, ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP003740; AGI66421.1; -; Genomic_DNA.
DR   AlphaFoldDB; M9R7Z0; -.
DR   STRING; 391626.OAN307_c06940; -.
DR   KEGG; oat:OAN307_c06940; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_018339_0_0_5; -.
DR   Proteomes; UP000005307; 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          71..502
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   DOMAIN          552..767
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   796 AA;  85098 MW;  1312E60B02EA0917 CRC64;
     MNGNSNITSR AAIPPVGVTR LDNDMTVKEI FDSMDYGPAP ESSAEALAWL ADRGGIAGHY
     INGKWDALRD DFPSNNPATG EKLAGVTKGT ADEVAKAVAA ARKAQPKWAK DGAARARVLY
     GIARLMQKNA RLLAVMETLD NGKPIRESRD IDIPLAIRHF YHHAGFAQLM DAEMPDVEPL
     GVCGQIIPWN FPLLMLAWKI APALAMGNTV VLKPAEYTSL SSMVFSEICT AAGVPPGVVN
     IITGDGETGA ALVDADVDKV AFTGSTSVGR IIREQTAGSG KALSLELGGK SPYIVFEDAD
     IDSAIEGLVD AIWFNSGQVC CAGSRLLVQE GIADRFYAKL RRRMDGLRIG DPMDKCIDLG
     AIVDPEQLAQ IKAMVDANTA GETYQCAAPE GCFYPPTLIT GLAPSDTLMQ EEIFGPVLVA
     CTFRTPAEAV EIANNTRYGL AASVWTENIN LALDIAPKLI AGIVWVNATN LMDAAAGFGG
     VRESGFGREG GWEGLMGYTK PKGKTAKITA PMPFTTQDGT PADPLDRTAK LYIGGKQVRP
     DSGYTQPIFD KSGKLLGHAS TANRKDLRNA VESNAAAKGW SKSTGHLRAQ ILYYIGENLS
     ARAQEFATRI NQLTGGRTGS KEVDDAISWL FTWAAWADKH DGAAKGVPIR GVALGMHEPV
     GNIAILTDDT RPLMGLIEPL APALAMGNRV TAVASQAFPL AATDFYQVLE TSDLPAGVAN
     ILTGRHTELA PHMAAHANID AVWSFSTADV SKVIETKSTS NLKRTWVNHA THRDWPSTIW
     RAQSTAIKTI WIPYGE
//
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