BETB_BURP1
ID BETB_BURP1 Reviewed; 489 AA.
AC Q3JLL8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Betaine aldehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00804};
DE Short=BADH {ECO:0000255|HAMAP-Rule:MF_00804};
DE EC=1.2.1.8 {ECO:0000255|HAMAP-Rule:MF_00804};
GN Name=betB {ECO:0000255|HAMAP-Rule:MF_00804};
GN OrderedLocusNames=BURPS1710b_A0376;
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
RN [2] {ECO:0007744|PDB:6WSB}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH NAD.
RA Edwards T.E., Dranow D.M., Abendroth J., Horanyi P.S., Lorimer D.D.;
RT "Crystal structure of a betaine aldehyde dehydrogenase from Burkholderia
RT pseudomallei bound to cofactor NAD.";
RL Submitted (APR-2020) to the PDB data bank.
CC -!- FUNCTION: Involved in the biosynthesis of the osmoprotectant glycine
CC betaine. Catalyzes the irreversible oxidation of betaine aldehyde to
CC the corresponding acid. {ECO:0000255|HAMAP-Rule:MF_00804}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.8; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00804};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15306;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00804};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00804};
CC Note=Binds 2 potassium ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00804};
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC choline pathway; betaine from betaine aldehyde: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00804}.
CC -!- SUBUNIT: Dimer of dimers. {ECO:0000255|HAMAP-Rule:MF_00804}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00804}.
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DR EMBL; CP000125; ABA51910.1; -; Genomic_DNA.
DR RefSeq; WP_004528662.1; NC_007435.1.
DR PDB; 6WSA; X-ray; 2.05 A; A=1-489.
DR PDB; 6WSB; X-ray; 1.55 A; A/B=1-489.
DR PDBsum; 6WSA; -.
DR PDBsum; 6WSB; -.
DR AlphaFoldDB; Q3JLL8; -.
DR SMR; Q3JLL8; -.
DR EnsemblBacteria; ABA51910; ABA51910; BURPS1710b_A0376.
DR GeneID; 56530225; -.
DR KEGG; bpm:BURPS1710b_A0376; -.
DR HOGENOM; CLU_005391_0_0_4; -.
DR OMA; AFTASMH; -.
DR OrthoDB; 744602at2; -.
DR UniPathway; UPA00529; UER00386.
DR Proteomes; UP000002700; Chromosome II.
DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR HAMAP; MF_00804; 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 InterPro; IPR011264; BADH.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01804; BADH; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; NAD; NADP; Oxidation; Oxidoreductase;
KW Potassium.
FT CHAIN 1..489
FT /note="Betaine aldehyde dehydrogenase"
FT /id="PRO_1000047038"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT ACT_SITE 251
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT ACT_SITE 285
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT ACT_SITE 463
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 26
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 93
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 150..152
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804,
FT ECO:0007744|PDB:6WSB"
FT BINDING 176..179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804,
FT ECO:0007744|PDB:6WSB"
FT BINDING 180
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 229..232
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804,
FT ECO:0007744|PDB:6WSB"
FT BINDING 245
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 253
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804,
FT ECO:0007744|PDB:6WSB"
FT BINDING 285
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /note="covalent"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804,
FT ECO:0007744|PDB:6WSB"
FT BINDING 386
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804,
FT ECO:0007744|PDB:6WSB"
FT BINDING 456
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 459
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT SITE 247
FT /note="Seems to be a necessary countercharge to the
FT potassium cations"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT MOD_RES 285
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:6WSB"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:6WSB"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:6WSB"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:6WSB"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:6WSB"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:6WSB"
FT HELIX 43..62
FT /evidence="ECO:0007829|PDB:6WSB"
FT HELIX 65..81
FT /evidence="ECO:0007829|PDB:6WSB"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:6WSB"
FT HELIX 98..103
FT /evidence="ECO:0007829|PDB:6WSB"
FT HELIX 105..119
FT /evidence="ECO:0007829|PDB:6WSB"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:6WSB"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:6WSB"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:6WSB"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:6WSB"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:6WSB"
FT HELIX 155..168
FT /evidence="ECO:0007829|PDB:6WSB"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:6WSB"
FT HELIX 184..195
FT /evidence="ECO:0007829|PDB:6WSB"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:6WSB"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:6WSB"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:6WSB"
FT HELIX 230..244
FT /evidence="ECO:0007829|PDB:6WSB"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:6WSB"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:6WSB"
FT HELIX 266..278
FT /evidence="ECO:0007829|PDB:6WSB"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:6WSB"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:6WSB"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:6WSB"
FT HELIX 298..310
FT /evidence="ECO:0007829|PDB:6WSB"
FT HELIX 330..346
FT /evidence="ECO:0007829|PDB:6WSB"
FT STRAND 349..352
FT /evidence="ECO:0007829|PDB:6WSB"
FT HELIX 360..364
FT /evidence="ECO:0007829|PDB:6WSB"
FT STRAND 371..375
FT /evidence="ECO:0007829|PDB:6WSB"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:6WSB"
FT STRAND 389..398
FT /evidence="ECO:0007829|PDB:6WSB"
FT HELIX 400..408
FT /evidence="ECO:0007829|PDB:6WSB"
FT STRAND 414..419
FT /evidence="ECO:0007829|PDB:6WSB"
FT HELIX 423..432
FT /evidence="ECO:0007829|PDB:6WSB"
FT STRAND 436..441
FT /evidence="ECO:0007829|PDB:6WSB"
FT HELIX 456..458
FT /evidence="ECO:0007829|PDB:6WSB"
FT STRAND 459..461
FT /evidence="ECO:0007829|PDB:6WSB"
FT HELIX 465..470
FT /evidence="ECO:0007829|PDB:6WSB"
FT STRAND 473..481
FT /evidence="ECO:0007829|PDB:6WSB"
SQ SEQUENCE 489 AA; 52191 MW; B53067B29C8665F5 CRC64;
MSVYGLQRLY IAGAHADATS GKTFDTFDPA TGELLARVQQ ASADDVDRAV ASAREGQREW
AAMTAMQRSR ILRRAVELLR ERNDALAELE MRDTGKPIAE TRAVDIVTGA DVIEYYAGLA
TAIEGLQVPL RPESFVYTRR EPLGVCAGIG AWNYPIQIAC WKSAPALAAG NAMIFKPSEV
TPLSALKLAE IYTEAGVPAG VFNVVQGDGS VGALLSAHPG IAKVSFTGGV ETGKKVMSLA
GASSLKEVTM ELGGKSPLIV FDDADLDRAA DIAVTANFFS AGQVCTNGTR VFVQQAVKDA
FVERVLARVA RIRVGKPSDS DTNFGPLASA AQLDKVLGYI DSGKAEGAKL LAGGARLVND
HFASGQYVAP TVFGDCRDDM RIVREEIFGP VMSILSFETE DEAIARANAT DYGLAAGVVT
ENLSRAHRAI HRLEAGICWI NTWGESPAEM PVGGYKQSGV GRENGITTLE HYTRIKSVQV
ELGRYQPVF
