ID C9ZQX6_TRYB9 Unreviewed; 543 AA.
AC C9ZQX6;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN ORFNames=TbgDal_VI2840 {ECO:0000313|EMBL:CBH11806.1};
OS Trypanosoma brucei gambiense (strain MHOM/CI/86/DAL972).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=679716 {ECO:0000313|EMBL:CBH11806.1, ECO:0000313|Proteomes:UP000002316};
RN [1] {ECO:0000313|Proteomes:UP000002316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/CI/86/DAL972 {ECO:0000313|Proteomes:UP000002316};
RX PubMed=20404998; DOI=10.1371/journal.pntd.0000658;
RA Jackson A.P., Sanders M., Berry A., McQuillan J., Aslett M.A., Quail M.A.,
RA Chukualim B., Capewell P., MacLeod A., Melville S.E., Gibson W.,
RA Barry J.D., Berriman M., Hertz-Fowler C.;
RT "The genome sequence of Trypanosoma brucei gambiense, causative agent of
RT chronic human african trypanosomiasis.";
RL PLoS Negl. Trop. Dis. 4:E658-E658(2010).
RN [2] {ECO:0007829|PDB:5NNO}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-543 IN COMPLEX WITH NAD(+).
RX PubMed=29425238; DOI=10.1371/journal.ppat.1006850;
RA Zhang N., Zoltner M., Leung K.F., Scullion P., Hutchinson S.,
RA Del Pino R.C., Vincent I.M., Zhang Y.K., Freund Y.R., Alley M.R.K.,
RA Jacobs R.T., Read K.D., Barrett M.P., Horn D., Field M.C.;
RT "Host-parasite co-metabolic activation of antitrypanosomal aminomethyl-
RT benzoxaboroles.";
RL PLoS Pathog. 14:e1006850-e1006850(2018).
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; FN554969; CBH11806.1; -; Genomic_DNA.
DR RefSeq; XP_011774091.1; XM_011775789.1.
DR PDB; 5NNO; X-ray; 2.50 A; A/B=2-543.
DR PDBsum; 5NNO; -.
DR AlphaFoldDB; C9ZQX6; -.
DR SMR; C9ZQX6; -.
DR GeneID; 23861932; -.
DR KEGG; tbg:TbgDal_VI2840; -.
DR VEuPathDB; TriTrypDB:Tbg972.6.2840; -.
DR OrthoDB; 606537at2759; -.
DR Proteomes; UP000002316; Chromosome 6.
DR GO; GO:0000166; F:nucleotide 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 GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR CDD; cd07087; ALDH_F3-13-14_CALDH-like; 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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:5NNO};
KW Nucleotide-binding {ECO:0007829|PDB:5NNO};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR036492,
KW ECO:0000256|RuleBase:RU003345}.
FT DOMAIN 11..453
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 220
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 256
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
FT BINDING 122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007829|PDB:5NNO"
FT BINDING 124
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007829|PDB:5NNO"
FT BINDING 148
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007829|PDB:5NNO"
FT BINDING 151
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007829|PDB:5NNO"
FT BINDING 220
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007829|PDB:5NNO"
FT BINDING 221
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007829|PDB:5NNO"
FT BINDING 362
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007829|PDB:5NNO"
SQ SEQUENCE 543 AA; 59705 MW; 2D0CA68BFD7F21C4 CRC64;
MPAGVPENTS LENIPVIVSK CREAFNDDAN RDLKKRKQVL RSLLNLVEEN TDEFCKAIHR
DRRRHRDETV VMEILPLRNE VWHLIEHMDE YVKPVKPTME GAAALDDCEL QYEPLGVVLV
IGTWNYPLLL ILQPLLGALA AGNTAVIKPS ELAPATAELL TKLLPKYVSS DVVGIVNGGV
SETTAVLKER FDHILYTGSA RVAEIVMAAA AKHLTPVTLE LGGKSPVVVD DTCADNMKVV
AERIMWGKII NAGQTCIAPD YVVVEKSMES VLVDALAEAR KAMLGDKFLK VLKGELLVKQ
KQQFLEESDY PRIVNASHFQ RLMEFMKGGK VAVGGEADEA TLTIAPTILT NIDPTHPVMQ
EEIFGPILPV LTYENEKDIL KIINSREKPL SLYVFSNNKR FIRGVESRTS SGAVVVNDVV
VHAGADGLPF GGVGRSGMGA YHGRYSFETF SHRRPVMRRG FLFSSIDTVR FPPYTTAKSR
VLNSLLKPSA EVAGAVGRSV WGVAALARVV EVGYHYMRFL MAGETTPAPS SSEPFSKSPR
SNE
//
