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Database: UniProt/TrEMBL
Entry: A8G2Z2_PROM2
LinkDB: A8G2Z2_PROM2
Original site: A8G2Z2_PROM2 
ID   A8G2Z2_PROM2            Unreviewed;       463 AA.
AC   A8G2Z2;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   24-JAN-2024, entry version 83.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN   OrderedLocusNames=P9215_03571 {ECO:0000313|EMBL:ABV49973.1};
OS   Prochlorococcus marinus (strain MIT 9215).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=93060 {ECO:0000313|EMBL:ABV49973.1, ECO:0000313|Proteomes:UP000002014};
RN   [1] {ECO:0000313|EMBL:ABV49973.1, ECO:0000313|Proteomes:UP000002014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9215 {ECO:0000313|EMBL:ABV49973.1,
RC   ECO:0000313|Proteomes:UP000002014};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492}.
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DR   EMBL; CP000825; ABV49973.1; -; Genomic_DNA.
DR   RefSeq; WP_012007123.1; NC_009840.1.
DR   AlphaFoldDB; A8G2Z2; -.
DR   STRING; 93060.P9215_03571; -.
DR   KEGG; pmh:P9215_03571; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_3_1_3; -.
DR   OMA; RHGKRWM; -.
DR   OrthoDB; 9762913at2; -.
DR   Proteomes; UP000002014; 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          30..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;  52629 MW;  F0430FB6B85C8A9F CRC64;
     MKSSDKFHLE DIYKLKNTVI TGKTEDIKWR IKQINIVSKL LDENKKEIIK SLFIDLGKSE
     IEGLSEILLV KEEISLIKKK LNSWMRPKEI DTPFYLFPSS SKIIYEPLGC VLILGPYNYP
     LLYVLKPLVN IFSAGNTAVI KPSEKCPATS KLIKKLTSKY FHKEVLLTVE GDYKQSIKLV
     EQHFDHIFFT GSTKTGKSIM KLASKNLTPL TLELSGTNPV IIFKNANLEV AAKRIVWGKF
     FNSGQSCVAP NHIFVDKEIE NNFIEKLKKC ILSFYGENPI TSENLSKLEK KQFSSTVEIL
     KRYKKEKRIL YGGTFNKKTL KISPTIMKAK LDETDILQKE LFSSLLPVIG IKNKESALEQ
     INQTSKPLAI YLFGGNKKIH NHISKVTSSG SICINDVMLP VLIPNLPFGG VGKSGIGKFH
     GEEGFRNFSN QKSITFKGFL FDLDLRYPPY ERIKKFLKIV FKI
//
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