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Database: UniProt
Entry: K6YJF9_9ALTE
LinkDB: K6YJF9_9ALTE
Original site: K6YJF9_9ALTE 
ID   K6YJF9_9ALTE            Unreviewed;       464 AA.
AC   K6YJF9;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN   ORFNames=GLIP_4137 {ECO:0000313|EMBL:GAC16748.1};
OS   Aliiglaciecola lipolytica E3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Aliiglaciecola.
OX   NCBI_TaxID=1127673 {ECO:0000313|EMBL:GAC16748.1, ECO:0000313|Proteomes:UP000006334};
RN   [1] {ECO:0000313|EMBL:GAC16748.1, ECO:0000313|Proteomes:UP000006334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E3 {ECO:0000313|EMBL:GAC16748.1,
RC   ECO:0000313|Proteomes:UP000006334};
RX   PubMed=25009843;
RA   Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA   Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT   "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT   high degree of genomic diversity and genomic characteristic for cold
RT   adaptation.";
RL   Environ. Microbiol. 16:1642-1653(2014).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492,
CC       ECO:0000256|RuleBase:RU003345}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAC16748.1}.
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DR   EMBL; BAEN01000076; GAC16748.1; -; Genomic_DNA.
DR   RefSeq; WP_008846550.1; NZ_BAEN01000076.1.
DR   AlphaFoldDB; K6YJF9; -.
DR   STRING; 1127673.GLIP_4137; -.
DR   eggNOG; COG1012; Bacteria.
DR   OrthoDB; 9812625at2; -.
DR   Proteomes; UP000006334; Unassembled WGS sequence.
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR036492};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006334}.
FT   DOMAIN          29..436
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        218
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        252
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ   SEQUENCE   464 AA;  51271 MW;  A4C88F200B4E1B11 CRC64;
     MNAADPTNHS EIANLVSGVR DTFASGYSKD YAWRVEQLKQ LELMIKEKQD DLLSALHTDL
     GKCKTEAWIS ELGFVLSDIN HTIKHLKKWM KPRKKSTPIG AQPGKSYVLP EPLGTVLIIG
     AWNYPFQLLI APLVAAIAAG NCAVLKPSEL SSHMSTLLAQ LIPKYLDNNA YVVVEGAVDE
     TTELLKQQFD HIFYTGGEAV GKIVMSAAAK HLTPVTLELG GKSPCIVDNS ANIDVTAARI
     VWSKWMNAGQ TCVAPDYVLV EKSISDQLVI AIQNKISDFY GKKPETSKDY GKIINERHFQ
     RLTGYLENQN VVFGGNQNIQ TGFFEPTLVL DPALDSTIMQ EEIFGPILPI ITLDSIDEAI
     PMVNARAKPL ALYVYTDSND YEQKVLQQTS AGNVCVNDGF MFMTNPDLPF GGVGNSGMGS
     YHGQSGFDRL SHLKTVMKRS FKFDVSLRYP PFSKFKLSIL KRVL
//
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