ID A0A176VUM8_MARPO Unreviewed; 481 AA.
AC A0A176VUM8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Aldehyde dehydrogenase domain-containing protein {ECO:0000259|Pfam:PF00171};
GN ORFNames=AXG93_1615s1580 {ECO:0000313|EMBL:OAE24504.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE24504.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE24504.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE24504.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC choline pathway; betaine from betaine aldehyde: step 1/1.
CC {ECO:0000256|ARBA:ARBA00037921}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, 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:OAE24504.1}.
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DR EMBL; LVLJ01002594; OAE24504.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VUM8; -.
DR OrthoDB; 3078548at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProt.
DR GO; GO:0070887; P:cellular response to chemical stimulus; IEA:UniProt.
DR CDD; cd07110; ALDH_F10_BADH; 1.
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; PTHR43860; BETAINE ALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43860:SF2; BETAINE ALDEHYDE DEHYDROGENASE-RELATED; 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|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT DOMAIN 233..463
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 238
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 481 AA; 52692 MW; 03E12EC2915096A1 CRC64;
MAPGIPSRQL FIGGEWVVPV RGERIPVICP TTELQIGDIP AATTEDVDIA VKAAREAFAR
NKGQDWSRAS GKHRAKYLRA IAAKVLERKE ELARFESLDC GKPIDEANWD MDDVSGCFEY
YADLAEKLDE RQYSPIELPM EQFKSSILRE ALGVVALITP WNYPLLMATW KVAAALAAGC
TAILKPSEMA SVTCLELGAI AKEVGLPPGV LNIITGLGTA AGAPLSSHQG VDKPVTLELG
GKSPIIIFDD ADVDSAVEWA MFGAFWTNGQ ICSATSRLLL QEGIASEFLR KLATWASSIK
ISDPLEKDCR LGPLVSDSQY KKVMNYIKVA QEEGANLVCG GKRPANMEKG YFVEATVLSD
VKPSMQIWRE EVFGPVLTVT TFKTEEEAIE LANDTEYGLG GAVISKDDER CKRVSELLQA
GIVWINCSQP CFSQAPWGGN KRSGFGRELG EWGLENYLSV KQITRYISDD KWGWYPVPSK
L
//
