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Database: UniProt
Entry: D5SVX9_PLAL2
LinkDB: D5SVX9_PLAL2
Original site: D5SVX9_PLAL2 
ID   D5SVX9_PLAL2            Unreviewed;       480 AA.
AC   D5SVX9;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   SubName: Full=Aldehyde Dehydrogenase {ECO:0000313|EMBL:ADG69489.1};
GN   OrderedLocusNames=Plim_3677 {ECO:0000313|EMBL:ADG69489.1};
OS   Planctopirus limnophila (strain ATCC 43296 / DSM 3776 / IFAM 1008 / Mu 290)
OS   (Planctomyces limnophilus).
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Planctopirus.
OX   NCBI_TaxID=521674 {ECO:0000313|EMBL:ADG69489.1, ECO:0000313|Proteomes:UP000002220};
RN   [1] {ECO:0000313|EMBL:ADG69489.1, ECO:0000313|Proteomes:UP000002220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43296 / DSM 3776 / IFAM 1008 / 290
RC   {ECO:0000313|Proteomes:UP000002220};
RX   PubMed=21304691; DOI=10.4056/sigs.1052813;
RA   Labutti K., Sikorski J., Schneider S., Nolan M., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Tindall B.J., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Planctomyces limnophilus type strain (Mu
RT   290).";
RL   Stand. Genomic Sci. 3:47-56(2010).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986}.
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DR   EMBL; CP001744; ADG69489.1; -; Genomic_DNA.
DR   RefSeq; WP_013111920.1; NC_014148.1.
DR   AlphaFoldDB; D5SVX9; -.
DR   STRING; 521674.Plim_3677; -.
DR   KEGG; plm:Plim_3677; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_0_0; -.
DR   OMA; VNGNWID; -.
DR   OrthoDB; 4503395at2; -.
DR   Proteomes; UP000002220; 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   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; PTHR42991; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42991:SF1; ALDEHYDE DEHYDROGENASE; 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:UP000002220}.
FT   DOMAIN          21..475
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   480 AA;  51661 MW;  40E4FDA8BE8E3707 CRC64;
     MSFIPVCLPL YIAGEPLVTS QPLEVRYPYD GSLTGTVSTA RHEHLEAAIQ AALKGHAPLS
     RYSREQVLRR ASLIFSQRTE EFARLMTRET GLALKDTRAE ASRVCDVLHG ASMAAMECDD
     ATFWGDVTPP GKILGSRNRS VHVMREPLRL AAAITPFNHP LTQLAHKVAP AIAAGTPIIL
     KPSDKTPLTA VRFAETLYEA GLPGWMLSVL IGPVDTVIEP LITDPRVEAI SFTGSVAVGK
     RIAGMAGYKR VCLELGGNSE LIVLKDADLA LAAKLACEGS YRNSGQRCTA VKRVLAEESI
     YEELAQRITE ATKAFMSGDP EDSKTDVGTL ISESAAIGIE KSLHEAMARG AVLLTGGQRN
     VALLAPTVLK DVPRDAPLVV EETFGPVTPI IPVRDLADAI QYANSSRYGL STSVVTDSMS
     QAMTAIRELH TGMVHVNEVP GYRLEQAPFG GIKDSGLGIK EGIIEAKKFY SNSKTYSLPW
//
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