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Database: UniProt
Entry: C6WGV6_ACTMD
LinkDB: C6WGV6_ACTMD
Original site: C6WGV6_ACTMD 
ID   C6WGV6_ACTMD            Unreviewed;       452 AA.
AC   C6WGV6;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:ACU36024.1};
GN   OrderedLocusNames=Amir_2078 {ECO:0000313|EMBL:ACU36024.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064
OS   / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU36024.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU36024.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 /
RC   NRRL B-12336 / IMRU 3971 / 101 {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L.,
RA   Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., Mavromatis K.,
RA   Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA   Detter J.C., Han C., Chain P., Tindall B.J., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP001630; ACU36024.1; -; Genomic_DNA.
DR   RefSeq; WP_015800913.1; NC_013093.1.
DR   AlphaFoldDB; C6WGV6; -.
DR   STRING; 446462.Amir_2078; -.
DR   KEGG; ami:Amir_2078; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_0_11; -.
DR   OrthoDB; 6882680at2; -.
DR   Proteomes; UP000002213; 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; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR11699:SF307; GAMMA-AMINOBUTYRALDEHYDE DEHYDROGENASE; 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:UP000002213}.
FT   DOMAIN          4..448
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        229
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   452 AA;  48137 MW;  FABDA4642EA82121 CRC64;
     MTALELINPA TGERVGEVEA ASVELVDAAI ARASAALPAW RAVSPADRSR LLRRFADAVD
     GAREELALLE VRNSGHTIGN ARWEAGNVRD VLHYYAAAPE RLFGRQIPVP GGLNVTFQEP
     LGVVGVIVPW NFPMPVAAWG FAPALAAGNT VVLKPAELTP LTALRLAELA REAGIPEDVL
     QVVPGRGDVA GWRFVTHPDV RKVVFTGSPA VGRKIMAGCA EQVKRVTLEL GGKSANVVFA
     DADIEQAAAT APYGVFDNAG QDCCARSRIL VQENVFDRFM ELLEPAVRGV VVGDPLDEKT
     EMGPLISAAH RERVASYVPD GAPVAFRGSA PDGPGFWFPP TVLSPVAPTD RVVVEEVFGP
     VVVVLPFRDE EDAVRLANAG DLGLSGSIWT RDVGRALRVS RAVEAGNLSV NSHSSVRYWT
     PFGGFKQSGL GRELGPDALD AFTEVKNVFI AH
//
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