ID A2CBP6_PROM3 Unreviewed; 459 AA.
AC A2CBP6;
DT 20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 20-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN OrderedLocusNames=P9303_21711 {ECO:0000313|EMBL:ABM78906.1};
OS Prochlorococcus marinus (strain MIT 9303).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=59922 {ECO:0000313|EMBL:ABM78906.1, ECO:0000313|Proteomes:UP000002274};
RN [1] {ECO:0000313|EMBL:ABM78906.1, ECO:0000313|Proteomes:UP000002274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9303 {ECO:0000313|EMBL:ABM78906.1,
RC ECO:0000313|Proteomes:UP000002274};
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,
CC ECO:0000256|RuleBase:RU003345}.
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DR EMBL; CP000554; ABM78906.1; -; Genomic_DNA.
DR AlphaFoldDB; A2CBP6; -.
DR STRING; 59922.P9303_21711; -.
DR KEGG; pmf:P9303_21711; -.
DR HOGENOM; CLU_005391_3_1_3; -.
DR BioCyc; PMAR59922:G1G80-1898-MONOMER; -.
DR Proteomes; UP000002274; 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; IPR029510; Ald_DH_CS_GLU.
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; PS00687; ALDEHYDE_DEHYDR_GLU; 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 25..431
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 209
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 243
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ SEQUENCE 459 AA; 50171 MW; 5285AE47EE98A6E3 CRC64;
MLPENFLLSG LRKPVISGLT RPEAWRRKQL KQIEVLIEKH QDEVLDALAT DLGKPPTEAL
FELIALRGEL KLAQRQLSRW MQPRHVQVPL AHQPGQAEVI LDPLGCVLII GPWNYPFSLT
LQPLISALAA GNTAVLKPSE HAPATSRLIA HVIPQHFSSE VVQVIEGDGA IAAALIKQPF
DHIFFTGSGA IGQKVMAAAA EHLTPVTLEL GGKSPAIVID GADLSVTARR LVWGKGLNAG
QTCIAPDHLL IQEQLKQPLL QAMKGAITEL YGGDPLRSPH LAKIINDCHF QRLQHLLDQA
KQRGKVLSGG QIDPDQRRIA PTLIDVDKRD DPLMEEELFG PLLPVISVHS LNEALAEVRQ
QPKPLALYLF GGTHADQQQL LNTTSSGGVC FNDVVMHVGI PELPFGGVGA SGMGRYHGLA
GFETFSHQKS VLRRPFWLDL KLRYPPYKAN LAMLKKLLG
//
