ID   GEOB_CASDE              Reviewed;         478 AA.
AC   H1ZV37;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Geranial dehydrogenase;
DE            Short=GaDH;
DE            EC=1.2.1.86;
DE   AltName: Full=Geraniol oxidation pathway protein B;
GN   Name=geoB;
OS   Castellaniella defragrans (Alcaligenes defragrans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Castellaniella.
OX   NCBI_TaxID=75697;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-18, FUNCTION,
RP   CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, INDUCTION, GENE NAME, AND
RP   PATHWAY.
RC   STRAIN=DSM 12143 / 65Phen;
RX   PubMed=22286981; DOI=10.1128/aem.07226-11;
RA   Luddeke F., Wulfing A., Timke M., Germer F., Weber J., Dikfidan A.,
RA   Rahnfeld T., Linder D., Meyerdierks A., Harder J.;
RT   "Geraniol and geranial dehydrogenases induced in anaerobic monoterpene
RT   degradation by Castellaniella defragrans.";
RL   Appl. Environ. Microbiol. 78:2128-2136(2012).
CC   -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of geranial to
CC       geranic acid. Is involved in the anaerobic degradation of the
CC       monoterpene beta-myrcene. Seems to be specific for the trans-isomer
CC       geranial, since it does not act on the cis-isomer neral.
CC       {ECO:0000269|PubMed:22286981}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranial + H2O + NAD(+) = geranate + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:34351, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16980, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:67260; EC=1.2.1.86;
CC         Evidence={ECO:0000269|PubMed:22286981};
CC   -!- PATHWAY: Terpene metabolism; monoterpene degradation.
CC       {ECO:0000269|PubMed:22286981}.
CC   -!- INDUCTION: By the monoterpene phellandrene, but not by acetate.
CC       {ECO:0000269|PubMed:22286981}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; FR669447; CCF55023.1; -; Genomic_DNA.
DR   AlphaFoldDB; H1ZV37; -.
DR   SMR; H1ZV37; -.
DR   BioCyc; MetaCyc:MON-17745; -.
DR   UniPathway; UPA00137; -.
DR   GO; GO:0034832; F:geranial dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR   GO; GO:0071310; P:cellular response to organic substance; IDA:UniProtKB.
DR   GO; GO:0043694; P:monoterpene catabolic process; TAS:UniProtKB.
DR   GO; GO:0016098; P:monoterpenoid metabolic process; IDA:UniProtKB.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 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   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:22286981"
FT   CHAIN           2..478
FT                   /note="Geranial dehydrogenase"
FT                   /id="PRO_0000418649"
FT   ACT_SITE        252
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        286
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   BINDING         230..235
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            155
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   478 AA;  50637 MW;  3890AAA65A4C87C8 CRC64;
     MTIDHQHIFV GGQWIAPKST QRSNILNAST EELVGSVPKC NNEDMDRAVA AAREAMRSLA
     WAGLDGKGRA QHLRRFADAV ERRGQQLARS VSLQNGMPIN VADQLESAFV VSLLRYYASL
     AENLVEEEAR PSPTGSTTLV RRDPVGVVGA IIPWNFPVAL SIFKIAPALA AGCAVVVKPS
     SGTVLDSYVL AEAAAEAGLP PGVINWVPGD RGIGSHLVSH PGVDKVAFTG STSAGRIIAE
     ACARLLRPVT LELGGKSAAI VLEDADLDAL IRSLPMSSVL NNGQACFSCT RILAPAGRYD
     EVVDAIAGAV SAYSVGDALD RATVVGPMAS AAHRDSVQRY IELGTGEARL VVGGGRTSQD
     RGWFVQPTVF ADVDNRSRIA REEIFGPVLS IIRYEGEDEA VEIANDSEYG LGGTVWSTDH
     DHAVTIARRM ETGTVGINGY MPDLNAPFGG VKSSGMGREL GPESIGAYQR YKSVYLLG