ID Q1QCC7_PSYCK Unreviewed; 496 AA. AC Q1QCC7; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 27-MAR-2024, entry version 97. DE RecName: Full=aldehyde dehydrogenase (NAD(+)) {ECO:0000256|ARBA:ARBA00024226}; DE EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226}; GN OrderedLocusNames=Pcryo_0895 {ECO:0000313|EMBL:ABE74676.1}; OS Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378 OS / K5). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Psychrobacter. OX NCBI_TaxID=335284 {ECO:0000313|EMBL:ABE74676.1, ECO:0000313|Proteomes:UP000002425}; RN [1] {ECO:0000313|Proteomes:UP000002425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5 RC {ECO:0000313|Proteomes:UP000002425}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., RA Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Richardson P.; RT "Complete sequence of chromosome of Psychrobacter cryohalolentis K5."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000323; ABE74676.1; -; Genomic_DNA. DR RefSeq; WP_011513237.1; NC_007969.1. DR AlphaFoldDB; Q1QCC7; -. DR STRING; 335284.Pcryo_0895; -. DR KEGG; pcr:Pcryo_0895; -. DR eggNOG; COG1012; Bacteria. DR HOGENOM; CLU_005391_1_2_6; -. DR Proteomes; UP000002425; Chromosome. DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC. DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC. DR CDD; cd07130; ALDH_F7_AASADH; 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; IPR044638; ALDH7A1-like. DR PANTHER; PTHR43521; ALPHA-AMINOADIPIC SEMIALDEHYDE DEHYDROGENASE; 1. DR PANTHER; PTHR43521:SF1; ALPHA-AMINOADIPIC SEMIALDEHYDE DEHYDROGENASE; 1. DR Pfam; PF00171; Aldedh; 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|RuleBase:RU003345}. FT DOMAIN 19..478 FT /note="Aldehyde dehydrogenase" FT /evidence="ECO:0000259|Pfam:PF00171" FT ACT_SITE 252 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007" SQ SEQUENCE 496 AA; 53482 MW; 4F50EF98C183BDC2 CRC64; MIKQYMSAMG VDESQYQAGD FAVHSPIDGE VIGKVALHQV NDVDTQIQDA KKAFKEWRTV PAPKRGELVR ILGEVLREHK EDLGALVSLE AGKIKEEGLG EVQEMIDICD FAVGLSRQLY GLTIASERPG HHMRETWQPL GVIAVISAFN FPVAVWSWNT ALALVCGNPV IWKPSEKTPL TAIACQALFE KALAKFGDAP ANLSQLLLGE ADVGNALVEH KDVALVSATG STRMGRIVGP KVAERFGKSL LELGGNNAMI LTPSADLDLA LRGILFSAVG TAGQRCTTLR RLFVHESVKD DILPRVKAAY STVSIGHPLE GNLVGPLIDE DSFNNMQDAL SKARAAGGTV TGGERVLQDK YPNAYYVTPA IVEMDAQNDV VRHETFAPIL YVMTYTEFDE ALELQNDVPQ GLSSCVFTND LREAELFLSA RGSDCGIANV NIGTSGAEIG GAFGGEKETG GGRESGSDAW KNYMRRQTNT VNYSTELPLA QGINFG //