ID B2FNG3_STRMK Unreviewed; 469 AA.
AC B2FNG3;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN Name=calB {ECO:0000313|EMBL:CAQ47974.1};
GN OrderedLocusNames=Smlt4620 {ECO:0000313|EMBL:CAQ47974.1};
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ47974.1, ECO:0000313|Proteomes:UP000008840};
RN [1] {ECO:0000313|EMBL:CAQ47974.1, ECO:0000313|Proteomes:UP000008840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a {ECO:0000313|EMBL:CAQ47974.1,
RC ECO:0000313|Proteomes:UP000008840};
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492,
CC ECO:0000256|RuleBase:RU003345}.
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DR EMBL; AM743169; CAQ47974.1; -; Genomic_DNA.
DR RefSeq; WP_012481636.1; NC_010943.1.
DR AlphaFoldDB; B2FNG3; -.
DR EnsemblBacteria; CAQ47974; CAQ47974; Smlt4620.
DR KEGG; sml:Smlt4620; -.
DR PATRIC; fig|522373.3.peg.4354; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_3_6_6; -.
DR Proteomes; UP000008840; 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 GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR CDD; cd07133; ALDH_CALDH_CalB; 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 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; 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:UP000008840}.
FT DOMAIN 25..436
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 215
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 249
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ SEQUENCE 469 AA; 51178 MW; 54993160A186DE5C CRC64;
MTTTTPEDLP ALLHTLRSAW QSQRPSLDQR EADLRRLREA LKPRLDEMAQ AIAEDFGHRA
HVESKLADGM SVLSAIDHLR RHLRRWSKPQ RVGAGWRLWP ARAQLRPTPL GVVGVISPWN
YPVTLALVPL ATAIAAGNHV LLKPSEHTPR TSAFLADLLA SVFPPDRVAV VQGGADVAAA
VSSLPLDHLL FTGSTAVGRK VMAAAAEHLV PVTLELGGKS PAIVCSDFPL EKAAARLATG
KWFNAGQTCI APDYVLIDTA RQREFVQALQ QQVRERYGDF SDAGDYTRII NEGQYQRLQG
YLAQARERGV PVIPLAQVDA ARADRERLLV PTVVLDPPDD LDLMREEIFG PILPVRAYPD
LEAALADVLS RDRPLALYPF SHDTATVERI LGQVVAGGVT VNDTLLHFAA DGLPFGGVGA
SGMGAYHGRA GFDAMSKRLP VLWQSRWAAS DRLRPPYSKI AGLLKLLLR
//
