ID A0A1Q6WQI3_9GAMM Unreviewed; 795 AA.
AC A0A1Q6WQI3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:OLB15499.1};
GN ORFNames=AUH10_01560 {ECO:0000313|EMBL:OLB15499.1};
OS Gammaproteobacteria bacterium 13_2_20CM_66_19.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1805166 {ECO:0000313|EMBL:OLB15499.1, ECO:0000313|Proteomes:UP000186999};
RN [1] {ECO:0000313|EMBL:OLB15499.1, ECO:0000313|Proteomes:UP000186999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|PIRNR:PIRNR036490, 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:OLB15499.1}.
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DR EMBL; MNCZ01000015; OLB15499.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q6WQI3; -.
DR STRING; 1805166.AUH10_01560; -.
DR Proteomes; UP000186999; 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:UniProtKB-UniRule.
DR CDD; cd07111; ALDH_F16; 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; IPR011408; Aldehyde_DH.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR PANTHER; PTHR11699:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 2.
DR PIRSF; PIRSF036490; Aldedh_dupl; 1.
DR SUPFAM; SSF53720; ALDH-like; 2.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345}.
FT DOMAIN 44..489
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 544..759
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 269
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 795 AA; 86179 MW; 4146DE2CDCFE14DE CRC64;
MANTSVAEKF RSMEYGAAPE DPHNSLVWLD RFGRRFGHFI GGKWRAPAQG RYFATADPST
GEKIAEVAAG SAADVNAAVK AARAALPHWQ ALTPHARARF LYALARQVQK HSRRLAVLET
LDNGKPIRES RDIDIPLVAR HFYYHAGWAQ LLEREFPDYR PRGVVGQIIP WNFPLLMVAW
KIAPALAAGN TVVLKPAEFT PLTALAFAEL CSEVGLPPGV VNIVTGDGKT GAALVVHPDV
DKIAFTGSTE VGRAIRRATA DSHKKLSLEL GGKSPFVVFE DADLDSAVEG LVDGIWLNQG
QVCCAGSRLL MQESIAVPLT KKLQVRMAAL RVGAPLDKTT DIGAIVARVQ LERIEGLVAQ
GVAEGASCWQ PDVPLPARGL FYRPTLLTNV HPTSVVARTE IFGPVLAAMT FRTPAEAVEL
ANNTAYGLAA SVWSESVNVA LQVAAQIKAG VVWVNSTNMF DAACGFGGYR ESGFGREGGR
EGMREYLEPV WLLKAPPLRA RAARSRRRTQ AADAARVIDR TVKLYIGGKQ VRPDSGYSLE
CRSSTGALLG ETPLGNRKDI RNAVEAARRA QQWGSATTHQ RAQVLYYAAE NLTQRGQDVT
ARLAAVVGRK QAAEEVRLGV ERLFAYAAWA DKYEGVVHSP PFRSISVAMN EAIGTAGVIC
PPEAPLLGFL SLVLPLVTAG NCVVAVPSES YPLIAGDLYQ LFDTSDVPGG VINLVTGRPG
ELLQVLAEHD DVDAIWCYGE EKLCAVAKRL SAGNLKQVWT NEGRRINFFS AREGEGRWYL
DHAFQVKNIW VPYGE
//
