ID   A4FCA2_SACEN            Unreviewed;       507 AA.
AC   A4FCA2;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   02-SEP-2026, entry version 95.
DE   SubName: Full=Aldehyde dehydrogenase (NAD+) {ECO:0000313|EMBL:CAM01677.1};
DE            EC=1.2.1.3 {ECO:0000313|EMBL:CAM01677.1};
GN   Name=thcA {ECO:0000313|EMBL:CAM01677.1};
GN   OrderedLocusNames=SACE_2377 {ECO:0000313|EMBL:CAM01677.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAM01677.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAM01677.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; AM420293; CAM01677.1; -; Genomic_DNA.
DR   RefSeq; WP_011873663.1; NC_009142.1.
DR   AlphaFoldDB; A4FCA2; -.
DR   STRING; 405948.SACE_2377; -.
DR   GeneID; 306459182; -.
DR   KEGG; sen:SACE_2377; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_0_11; -.
DR   Proteomes; UP000006728; Chromosome.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   CDD; cd07559; ALDH_ACDHII_AcoD-like; 1.
DR   FunFam; 3.40.605.10:FF:000001; Aldehyde dehydrogenase 1; 1.
DR   FunFam; 3.40.309.10:FF:000012; Betaine aldehyde dehydrogenase; 1.
DR   Gene3D; 3.40.605.10; Aldehyde Dehydrogenase, Chain A, domain 1; 1.
DR   Gene3D; 3.40.309.10; Aldehyde Dehydrogenase, Chain A, domain 2; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   NCBIfam; NF050026; AcaldDHExaC; 1.
DR   PANTHER; PTHR43111; ALDEHYDE DEHYDROGENASE B-RELATED; 1.
DR   PANTHER; PTHR43111:SF1; ALDEHYDE DEHYDROGENASE B-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728}.
FT   DOMAIN          30..494
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        263
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        302
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10008"
SQ   SEQUENCE   507 AA;  54808 MW;  98F3278256BFCDAA CRC64;
     MVLYAAPGAA GSVVEYRSRY DHFIGGEYVA PAGGEYFENP TPVTGKTFTE IARGTADDVE
     RALDAAEGAA PAWGRTPAAE RAGVLLRIAD RMEHNLEKLA VAESWENGKP VRETLAADLP
     LAIDHFRYFA GALRAQEGSI SQIDEDTVAY HFHEPLGVVA QIIPWNFPLL MATWKLAPAL
     AAGNAVVLKP AEQTPASIHV LLDLIADLLP AGVLNVVNGF GVEAGKPLAS SPRVRKVAFT
     GETTTGRLIL QYASQNIIPV TVELGGKSPN IFFDDVAAQQ DAFYDKALEG FTMFALNQGE
     VCTCPSRALI QSGIYEGFLS DAVARTERIK QGNPLDTDTQ IGAQASNDQL EKILSYIDIG
     RQEGAEVLTG GHRVELEGDL AGGYYVAPTI FQGHNNQRIF QEEIFGPVVS VAKFDDYADA
     MNTANDTLYG LGAGVWSRNA GTAYRAGRDI QAGRVWVNNY HAYPAHAAFG GYKQSGIGRE
     THKMMLDHYQ QTKNMLVSYS DNALGFF
//