BETB_AGRFC
ID BETB_AGRFC Reviewed; 493 AA.
AC Q8UH56; Q7D0K9;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
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}; OrderedLocusNames=Atu0829;
GN ORFNames=AGR_C_1515;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), AND SUBUNIT.
RG New York structural genomics research consortium (NYSGRC);
RT "Crystal structure of betaine aldehyde dehydrogenase from Agrobacterium
RT tumefaciens.";
RL Submitted (MAR-2011) 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:0000305|Ref.3}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00804}.
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DR EMBL; AE007869; AAK86635.1; -; Genomic_DNA.
DR PIR; AE2678; AE2678.
DR PIR; B97460; B97460.
DR RefSeq; NP_353850.1; NC_003062.2.
DR RefSeq; WP_010971179.1; NC_003062.2.
DR PDB; 3R31; X-ray; 2.15 A; A/B=1-493.
DR PDBsum; 3R31; -.
DR AlphaFoldDB; Q8UH56; -.
DR SMR; Q8UH56; -.
DR STRING; 176299.Atu0829; -.
DR EnsemblBacteria; AAK86635; AAK86635; Atu0829.
DR KEGG; atu:Atu0829; -.
DR PATRIC; fig|176299.10.peg.825; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_2_5; -.
DR OMA; GMKYVTM; -.
DR PhylomeDB; Q8UH56; -.
DR BioCyc; AGRO:ATU0829-MON; -.
DR UniPathway; UPA00529; UER00386.
DR Proteomes; UP000000813; Chromosome circular.
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; Reference proteome.
FT CHAIN 1..493
FT /note="Betaine aldehyde dehydrogenase"
FT /id="PRO_0000056535"
FT ACT_SITE 168
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT ACT_SITE 256
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT ACT_SITE 290
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT ACT_SITE 467
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 32
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 33
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 99
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 156..158
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 182..185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 235..238
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 250
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 258
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 290
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /note="covalent"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 390
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 460
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 463
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT MOD_RES 290
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:3R31"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:3R31"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:3R31"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:3R31"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:3R31"
FT HELIX 49..68
FT /evidence="ECO:0007829|PDB:3R31"
FT HELIX 71..87
FT /evidence="ECO:0007829|PDB:3R31"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:3R31"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:3R31"
FT HELIX 112..129
FT /evidence="ECO:0007829|PDB:3R31"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:3R31"
FT STRAND 138..148
FT /evidence="ECO:0007829|PDB:3R31"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:3R31"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:3R31"
FT HELIX 161..174
FT /evidence="ECO:0007829|PDB:3R31"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:3R31"
FT HELIX 190..200
FT /evidence="ECO:0007829|PDB:3R31"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:3R31"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:3R31"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:3R31"
FT HELIX 236..248
FT /evidence="ECO:0007829|PDB:3R31"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:3R31"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:3R31"
FT HELIX 271..282
FT /evidence="ECO:0007829|PDB:3R31"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:3R31"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:3R31"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:3R31"
FT HELIX 303..316
FT /evidence="ECO:0007829|PDB:3R31"
FT HELIX 335..351
FT /evidence="ECO:0007829|PDB:3R31"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:3R31"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:3R31"
FT STRAND 375..380
FT /evidence="ECO:0007829|PDB:3R31"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:3R31"
FT STRAND 392..401
FT /evidence="ECO:0007829|PDB:3R31"
FT HELIX 404..412
FT /evidence="ECO:0007829|PDB:3R31"
FT STRAND 414..423
FT /evidence="ECO:0007829|PDB:3R31"
FT HELIX 427..436
FT /evidence="ECO:0007829|PDB:3R31"
FT STRAND 440..446
FT /evidence="ECO:0007829|PDB:3R31"
FT HELIX 470..475
FT /evidence="ECO:0007829|PDB:3R31"
FT STRAND 476..484
FT /evidence="ECO:0007829|PDB:3R31"
SQ SEQUENCE 493 AA; 52204 MW; 7636ADEEB5327833 CRC64;
MTIATPLKAQ PKASHFIDGD YVEDNTGTPF ESIFPATGEM IAKLHAATPA IVERAIASAK
RAQKEWAAMS PMARGRILKR AADIMRERND ALSTLETLDT GKPIQETIVA DPTSGADAFE
FFGGIAPSAL NGDYIPLGGD FAYTKRVPLG VCVGIGAWNY PQQIACWKAA PALVAGNAMV
FKPSENTPLG ALKIAEILIE AGLPKGLFNV IQGDRDTGPL LVNHPDVAKV SLTGSVPTGR
KVAAAAAGHL KHVTMELGGK SPMIVFDDAD IESAVGGAML GNFYSSGQVC SNGTRVFVQK
KAKARFLENL KRRTEAMILG DPLDYATHLG PLVSKAQQEK VLSYIEKGKA EGATLITGGG
IPNNVAGEGA YVQPTVFADV TDDMTIAREE IFGPVMCVLD FDDEDEVLAR ANATEFGLAG
GVFTADLARA HRVVDGLEAG TLWINTYNLC PVEIPFGGSK QSGFGRENSA AALEHYSELK
TVYVSTGKVD APY
