ID R7GSI0_9FIRM Unreviewed; 456 AA.
AC R7GSI0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN ORFNames=BN591_01241 {ECO:0000313|EMBL:CDE28897.1};
OS Catenibacterium sp. CAG:290.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Catenibacterium; environmental samples.
OX NCBI_TaxID=1262767 {ECO:0000313|EMBL:CDE28897.1, ECO:0000313|Proteomes:UP000018308};
RN [1] {ECO:0000313|EMBL:CDE28897.1, ECO:0000313|Proteomes:UP000018308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:290 {ECO:0000313|Proteomes:UP000018308};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492,
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:CDE28897.1}.
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DR EMBL; CBIQ010000134; CDE28897.1; -; Genomic_DNA.
DR AlphaFoldDB; R7GSI0; -.
DR STRING; 1262767.BN591_01241; -.
DR Proteomes; UP000018308; 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 GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
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 InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43570:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 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|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR036492};
KW Reference proteome {ECO:0000313|Proteomes:UP000018308}.
FT DOMAIN 3..427
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 209
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 243
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ SEQUENCE 456 AA; 51910 MW; 97C223A189AC3416 CRC64;
MDLEKIFNDQ KTYYDTLMTR DVSLRIDAIK RVKLWIKDHM DLIEDALEKD LGKSRGESYM
TEIGLTLEAC TYTLKNIKKW VKKEKVKTPL HQFFSRSYTI YEPYGVTLII SPWNYPFLLA
IEPLIGTIAA GNCAIVKPSE QTPHTSAIVA QLIDTCFDKG HAYCAEGGLE VSKELVDLPF
DYIFFTGGKK AGKEIYMKAA ETLTPVTLEL GGKSPAILTD MIPMEIAAKR IIFGKFLNAG
QTCIAPDYIL IKDSMKAAFI DYASEYIKKF FGEHPLESEN LCKIINKDQF DRLKKLLENQ
DILIGGEVDE EHLKIAPTIV NDVDFDNPLM EEEIFGPILP LVEYNRIEEA IQYINSHDKP
LALYLFSNDS YHANKILDLC SFGDACINDT VSHFATNTLP FGGVGASGIG YYHGKFTFET
FSHRRSVLHK STRIDLPFRY YPLTDDKMKW IKRFLK
//