GenomeNet

Database: UniProt
Entry: H6N2U5_GORPV
LinkDB: H6N2U5_GORPV
Original site: H6N2U5_GORPV 
ID   H6N2U5_GORPV            Unreviewed;       488 AA.
AC   H6N2U5;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:AFA74722.1};
GN   OrderedLocusNames=GPOL_c37100 {ECO:0000313|EMBL:AFA74722.1};
OS   Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA74722.1, ECO:0000313|Proteomes:UP000009154};
RN   [1] {ECO:0000313|EMBL:AFA74722.1, ECO:0000313|Proteomes:UP000009154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154};
RX   PubMed=22327575; DOI=10.1128/AEM.07969-11;
RA   Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., Angelov A.,
RA   Liebl W., Daniel R., Steinbuchel A.;
RT   "Involvement of two latex-clearing proteins during rubber degradation and
RT   insights into the subsequent degradation pathway revealed by the genome
RT   sequence of Gordonia polyisoprenivorans strain VH2.";
RL   Appl. Environ. Microbiol. 78:2874-2887(2012).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {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; CP003119; AFA74722.1; -; Genomic_DNA.
DR   RefSeq; WP_014361065.1; NC_016906.1.
DR   AlphaFoldDB; H6N2U5; -.
DR   STRING; 1112204.GPOL_c37100; -.
DR   KEGG; gpo:GPOL_c37100; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_0_11; -.
DR   OMA; AFTASMH; -.
DR   Proteomes; UP000009154; 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   CDD; cd07089; ALDH_CddD-AldA-like; 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; IPR026460; Aldehyde_dehydrogenase_Rv0768.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   NCBIfam; TIGR04284; aldehy_Rv0768; 1.
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   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009154}.
FT   DOMAIN          23..484
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        259
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   488 AA;  51017 MW;  741EE93794AB4610 CRC64;
     MSLRPVSASD LLIDGKLIPG GGGTFDVINP ATEAAIGKAA DADAADMDAA IAAARRAFDE
     TPWSRDHSFR ARCLRQLRDA LLAHVDELRD ITVAEVGCPV FLTHGPQLEG PINDLGYFAD
     LAENYSWTTD LGEAKPMGLK NHREVRSEAA GVVGAITPWN FPHQINFAKI GPALAAGCTV
     VLKPAPDTPW CAALVGKVIA EETDFPPGVV NIVTSSDHAV GAQLGSDPRV DVVSFTGSTA
     TGKKVMAAAA ESLTKVFLEL GGKSAFIVLD DADLAAACSM AAFAVVTHAG QGCAITTRLL
     VPRERLDEAI SATRDSLAGL AAGDPTDPGT ICGPLISARQ RQRVESYIEL ARAEGGTIEI
     GGGRPTDQPT GFFVEPTLIS GVDNSSRVAQ EEIFGPVLVI LPHDGDDDAI RIANDSPYGL
     SGAVWGTDED RINKVVNGIR TGTMSVNGGI WYSADVPFGG YKASGIGREM GVAGFEEYLQ
     TKAVARPA
//
DBGET integrated database retrieval system