ID   Q7V2X1_PROMP            Unreviewed;       463 AA.
AC   Q7V2X1;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN   OrderedLocusNames=PMM0331 {ECO:0000313|EMBL:CAE18790.1};
OS   Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS   MED4).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=59919 {ECO:0000313|EMBL:CAE18790.1, ECO:0000313|Proteomes:UP000001026};
RN   [1] {ECO:0000313|EMBL:CAE18790.1, ECO:0000313|Proteomes:UP000001026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1986 / NIES-2087 / MED4
RC   {ECO:0000313|Proteomes:UP000001026};
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492}.
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DR   EMBL; BX548174; CAE18790.1; -; Genomic_DNA.
DR   RefSeq; WP_011131968.1; NC_005072.1.
DR   AlphaFoldDB; Q7V2X1; -.
DR   STRING; 59919.PMM0331; -.
DR   KEGG; pmm:PMM0331; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_3_1_3; -.
DR   OrthoDB; 9762913at2; -.
DR   Proteomes; UP000001026; Chromosome.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR   CDD; cd07087; ALDH_F3-13-14_CALDH-like; 1.
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   InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR   PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43570:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR036492}.
FT   DOMAIN          27..434
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        213
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
FT   ACT_SITE        247
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ   SEQUENCE   463 AA;  52773 MW;  925D5FBA99F0CF1D CRC64;
     MNILDKSYKS NIEELKNKVI TGQTESISWR IQQIRKVSQL LDENKKEIIK ALFLDLGKSE
     LEALSEILLI KEEISLIKKN LRLWMRPKKV KTPIYLFPSF SKVIYEPLGC VLILGPYNYP
     LLYLLKPLVN IFSSGNTAVI KPSEKCSSTS KLIKKLTDKY FQKDILFTIE GDYKESIKLV
     EQNFDHIFFT GSTETGKSIM KSASTNLTPL TLELSGTNPV IIFKNANLEI AAKRIVWGKF
     FNSGQSCMAP NHIFVEKEIE NQLVKELKKF INIFYGEDPI ISKNLSKLEK KQFSITSELL
     KKYKKEKRIL FGGTCSKKRM KISPTILKVK LHDNNIIQKE LFSSLLPVIG IDNKDLALKK
     INQASKPLAI YIFGGNKKIH DHISKVTSSG TVCINDVMLP VLIPNLPFGG VGESGMGKFH
     GEEGFKNFSN QKSITYKGFL FDLDFRYPPY NKVMKIIKFI FKI
//