ID S6AQM0_PSERE Unreviewed; 490 AA.
AC S6AQM0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Betaine aldehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00804};
DE Short=BADH {ECO:0000256|HAMAP-Rule:MF_00804};
DE EC=1.2.1.8 {ECO:0000256|HAMAP-Rule:MF_00804};
GN Name=betB {ECO:0000256|HAMAP-Rule:MF_00804,
GN ECO:0000313|EMBL:BAN46126.1};
GN ORFNames=PCA10_03940 {ECO:0000313|EMBL:BAN46126.1};
OS Pseudomonas resinovorans NBRC 106553.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1245471 {ECO:0000313|EMBL:BAN46126.1, ECO:0000313|Proteomes:UP000015503};
RN [1] {ECO:0000313|EMBL:BAN46126.1, ECO:0000313|Proteomes:UP000015503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 106553 {ECO:0000313|EMBL:BAN46126.1,
RC ECO:0000313|Proteomes:UP000015503};
RX PubMed=23887915; DOI=10.1128/genomeA.00488-13;
RA Shintani M., Hosoyama A., Ohji S., Tsuchikane K., Takarada H., Yamazoe A.,
RA Fujita N., Nojiri H.;
RT "Complete Genome Sequence of the Carbazole Degrader Pseudomonas
RT resinovorans Strain CA10 (NBRC 106553).";
RL Genome Announc. 1:e00488-13(2013).
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:0000256|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:0000256|HAMAP-
CC Rule:MF_00804};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00804};
CC Note=Binds 2 potassium ions per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00804}.
CC -!- SUBUNIT: Dimer of dimers. {ECO:0000256|HAMAP-Rule:MF_00804}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|HAMAP-Rule:MF_00804, ECO:0000256|RuleBase:RU003345}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00804}.
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DR EMBL; AP013068; BAN46126.1; -; Genomic_DNA.
DR RefSeq; WP_016490337.1; NC_021499.1.
DR AlphaFoldDB; S6AQM0; -.
DR STRING; 1245471.PCA10_03940; -.
DR KEGG; pre:PCA10_03940; -.
DR PATRIC; fig|1245471.3.peg.388; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_2_6; -.
DR OrthoDB; 9812625at2; -.
DR UniPathway; UPA00529; UER00386.
DR Proteomes; UP000015503; Chromosome.
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 CDD; cd07090; ALDH_F9_TMBADH; 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 NCBIfam; TIGR01804; BADH; 1.
DR PANTHER; PTHR11699:SF228; 4-TRIMETHYLAMINOBUTYRALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 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 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00804};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00804};
KW NADP {ECO:0000256|HAMAP-Rule:MF_00804};
KW Oxidation {ECO:0000256|ARBA:ARBA00023097, ECO:0000256|HAMAP-Rule:MF_00804};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00804};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_00804};
KW Reference proteome {ECO:0000313|Proteomes:UP000015503}.
FT DOMAIN 15..479
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT ACT_SITE 252
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 252
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT ACT_SITE 286
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT ACT_SITE 464
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 26
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 27
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 93
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 150..152
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 176..179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 230..233
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 246
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 254
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 286
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 387
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 457
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 460
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT SITE 248
FT /note="Seems to be a necessary countercharge to the
FT potassium cations"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT MOD_RES 286
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
SQ SEQUENCE 490 AA; 53300 MW; 6646F183D480845A CRC64;
MARFEEQKLY IGGRYVDSSS GATFETINPA NGEVLASVQR AGKEDVERAV ASAIEGQKVW
AAMTAMQRSR ILRRAVDILR ERNDELAELE TLDTGKPLAE TRAVDIVTGA DVIEYYAGLI
PAIEGEQIPL RETSFVYTRR EPLGVVAGIG AWNYPVQIAM WKSAPALAAG NAMIFKPSEV
TPLTALKLAE IYTQAGVPDG VFNVLTGSGR EVGQWLTEHP QIEKISFTGG TSTGKKVMAS
ASSSSLKEVT MELGGKSPLI IFDDADLDRA ADIAVMANFF SSGQVCTNGT RVFVPRALQA
RFEAKVVERV KRIRLGNPQD AETNFGPLTS FAHMESVLGY IESGRKEGAR LLIGGERVTE
GEFAKGAYVS ATVFSDCTDD MTIVREEIFG PVMSILVYDT EEEVIRRAND TDYGLAAGVV
TRDLARAHRV IHKLEAGICW INTWGESPAE MPVGGYKQSG VGRENGLTTL AHYTRIKSVQ
VEMGDYFSVF
//
