ID   Q3MAW0_TRIV2            Unreviewed;       473 AA.
AC   Q3MAW0;
DT   25-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:ABA21876.1};
DE            EC=1.2.1.3 {ECO:0000313|EMBL:ABA21876.1};
GN   OrderedLocusNames=Ava_2258 {ECO:0000313|EMBL:ABA21876.1};
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Trichormus.
OX   NCBI_TaxID=240292 {ECO:0000313|EMBL:ABA21876.1, ECO:0000313|Proteomes:UP000002533};
RN   [1] {ECO:0007829|PDB:4H7N}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-471.
RA   Cuff M.E., Chhor G., Clancy S., Joachimiak A.;
RT   "The Structure of Putative Aldehyde Dehydrogenase PutA from Anabaena
RT   variabilis.";
RL   Submitted (SEP-2012) to the PDB data bank.
RN   [2] {ECO:0000313|Proteomes:UP000002533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937 {ECO:0000313|Proteomes:UP000002533};
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP000117; ABA21876.1; -; Genomic_DNA.
DR   PDB; 4H7N; X-ray; 2.00 A; A/B/C/D=1-471.
DR   PDBsum; 4H7N; -.
DR   AlphaFoldDB; Q3MAW0; -.
DR   SMR; Q3MAW0; -.
DR   STRING; 240292.Ava_2258; -.
DR   KEGG; ava:Ava_2258; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_0_3; -.
DR   Proteomes; UP000002533; 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; cd07099; ALDH_DDALDH; 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   PANTHER; PTHR42804; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42804:SF1; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4H7N};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345}.
FT   DOMAIN          3..451
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        229
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   473 AA;  51565 MW;  8F7C7FD63CDA155B CRC64;
     MTKTIEVRNP RTGKFDYVII PPPPRLLAQQ CNRARRAQSR WQELGVEGRI TTLQQWKQAI
     LSRREQLTEA LVNDTGRLSI TVLEIDSFLA SIDRWCGLAP ELLQTSAKNT SIPFIALQQS
     LVPYPLVGVI SPWNFPLTLS MIDTIPALLA GCAVVVKPSE IAPRFVAPLL MALNTVPELR
     DVLIFVEGGG ETGANLINYV DFVCFTGSVA TGREVAETAA RRFIPAYLEL GGKDPAIVLE
     SANLELATSA ILWGAVVNTG QSCLSIERIY VAESKFEEFY HQLIAKAHRL QLAYPLVEDG
     AIGPIIAEKQ AGIINDHILD AVEKGAVIHC GGKVEELGGG WWCRPTVMTN VNHSMKVMTE
     ETFGPIMPVM PFPDVEEAVY LANDTIYGLS AAVFAGSEDE ALKVARQLNA GAISINDAAL
     TAMMHEGEKN AFNFSGLGGS RVGAAGLKRF LRKQAFLIKT NSTSDPWWFD KGD
//