ID B4EFS9_BURCJ Unreviewed; 496 AA.
AC B4EFS9;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=2-aminomuconate 6-semialdehyde dehydrogenase {ECO:0000313|EMBL:CAR55990.1};
GN Name=nbaE {ECO:0000313|EMBL:CAR55990.1};
GN ORFNames=BCAM2132 {ECO:0000313|EMBL:CAR55990.1};
OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=216591 {ECO:0000313|EMBL:CAR55990.1, ECO:0000313|Proteomes:UP000001035};
RN [1] {ECO:0000313|EMBL:CAR55990.1, ECO:0000313|Proteomes:UP000001035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 /
RC CF5610 {ECO:0000313|Proteomes:UP000001035};
RX PubMed=18931103; DOI=10.1128/JB.01230-08;
RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT cystic fibrosis patients.";
RL J. Bacteriol. 191:261-277(2009).
RN [2] {ECO:0007829|PDB:4U3W}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 2-496 IN COMPLEX WITH MAGNESIUM.
RA Fairman J.W., Dranow D.M., Lorimer D., Edwards T.E.;
RT "X-ray crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase
RT from Burkholderia cenocepacia.";
RL Submitted (JUL-2014) to the PDB data bank.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM747721; CAR55990.1; -; Genomic_DNA.
DR RefSeq; WP_006490292.1; NC_011001.1.
DR PDB; 4U3W; X-ray; 1.95 A; A/B=2-496.
DR PDBsum; 4U3W; -.
DR AlphaFoldDB; B4EFS9; -.
DR SMR; B4EFS9; -.
DR KEGG; bcj:BCAM2132; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_0_4; -.
DR BioCyc; BCEN216591:G1G1V-6201-MONOMER; -.
DR Proteomes; UP000001035; Chromosome 2.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd07093; ALDH_F8_HMSADH; 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 InterPro; IPR017628; OHmuconic_semiald_DH.
DR NCBIfam; TIGR03216; OH_muco_semi_DH; 1.
DR PANTHER; PTHR43720; 2-AMINOMUCONIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43720:SF2; 2-AMINOMUCONIC SEMIALDEHYDE DEHYDROGENASE; 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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4U3W}; Metal-binding {ECO:0007829|PDB:4U3W};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345}.
FT DOMAIN 27..491
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 263
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
FT BINDING 33
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4U3W"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4U3W"
FT BINDING 277
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:4U3W"
FT BINDING 279
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:4U3W"
FT BINDING 483
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0007829|PDB:4U3W"
FT BINDING 486
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0007829|PDB:4U3W"
SQ SEQUENCE 496 AA; 53238 MW; 386E317D159D4715 CRC64;
MTTQLNSTSR DRQLLRHYIN GEFVASGTTF PNLSPVDGRK LADVCEADAA LVDSAVQAAH
AAQKAGWRDT TPAQRAAWLH KIADGIEARF DEFVAAEVAD TGRPVAQART LDIARGIANF
RTFADLVRTA SGEYFETHAA DGSELINYVT RKPLGVIGII SPWNLPLLLF TWKVAPALAM
GNCVVAKPSE ETPSSATLLA EVMHDVGLPP GVFNLIHGHG QNAAGEFLTR HPDISAITFT
GESRTGSTIM KAVADGVKEV SFELGGKNAA VVFADADFDA AVAGVLRSSF TNAGQVCLCS
ERVYVERPIF ERFVAALKEQ AQALRVGAPE DPATTMGPLI SRGHRDKVLS YFRLAVEEGA
TVVTGGGAPS FGDARDDGAF VMPTIWTGLP DSARCVREEI FGPVCHIAPF DDEAEVVKRV
NDSAYGLAAS IWTTQLARGH RVAKQIETGI VWVNAWFVRD LRTPFGGTKL SGLGREGGRH
SLDFYSELTN VCVRIA
//
