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Database: UniProt
Entry: R4Z5L4_9ACTN
LinkDB: R4Z5L4_9ACTN
Original site: R4Z5L4_9ACTN 
ID   R4Z5L4_9ACTN            Unreviewed;       473 AA.
AC   R4Z5L4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Medium chain aldehyde dehydrogenase {ECO:0000313|EMBL:CCM64626.1};
GN   Name=ydcW {ECO:0000313|EMBL:CCM64626.1};
GN   ORFNames=BN381_430022 {ECO:0000313|EMBL:CCM64626.1};
OS   Candidatus Microthrix parvicella RN1.
OC   Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC   Microthrixaceae; Microthrix.
OX   NCBI_TaxID=1229780 {ECO:0000313|EMBL:CCM64626.1, ECO:0000313|Proteomes:UP000018291};
RN   [1] {ECO:0000313|EMBL:CCM64626.1, ECO:0000313|Proteomes:UP000018291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RN1 {ECO:0000313|EMBL:CCM64626.1,
RC   ECO:0000313|Proteomes:UP000018291};
RX   PubMed=23446830; DOI=10.1038/ismej.2013.6;
RA   Jon McIlroy S., Kristiansen R., Albertsen M., Michael Karst S.,
RA   Rossetti S., Lund Nielsen J., Tandoi V., James Seviour R., Nielsen P.H.;
RT   "Metabolic model for the filamentous 'Candidatus Microthrix parvicella'
RT   based on genomic and metagenomic analyses.";
RL   ISME J. 7:1161-1172(2013).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
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:CCM64626.1}.
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DR   EMBL; CANL01000038; CCM64626.1; -; Genomic_DNA.
DR   RefSeq; WP_012228840.1; NZ_HG422565.1.
DR   AlphaFoldDB; R4Z5L4; -.
DR   STRING; 1229780.BN381_430022; -.
DR   GeneID; 78314419; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_2_11; -.
DR   OrthoDB; 6882680at2; -.
DR   Proteomes; UP000018291; 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   CDD; cd07092; ALDH_ABALDH-YdcW; 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; IPR015657; Aminobutyraldehyde_DH.
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; 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:UP000018291}.
FT   DOMAIN          11..469
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        246
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   473 AA;  50248 MW;  8981FF59EA5AADFB CRC64;
     MAMQNYIGGE WRDAASRGTD EVLNPATGEC ITEVAASDAD DVDAAVAAAT DAFVSWGRTS
     PRERSEKLLA LADAVEDNLD ELKRLEMENV GKPTSIIEFE FDLTVDNLRF FAGAARTMNT
     QAAGEYIEDH TSMLRRDPLG VCAGIAPWNY PLNMAVWKLG PALAAGNTFI LKPSELTPMT
     ALKLAEISAD IFPPGVFNVV TGQGETAGDA LVKHPGVAMV SITGDVDTGK LIARNAADSL
     KRVHLELGGK APVVVFDDAD LETLVATLAE TGYYNSGQDC TAPCRVVAGP RIYDDLVAGL
     SSAVGDLVTG DPMDEATAVG PLVSAGQQAR VAGMVGRAVE GGAEVTVGGD TLDRAGFFYA
     PTVVANPAQD AEIVQREVFG PVISVQRFSD DDQALAWANG VNYGLAASVW TSDVSRAMRM
     SAHLRFGTVW VNDHIPIVSE MPHGGFKQSG YGKDMSIYAV EHYTELKHVM VKF
//
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