ID F9TB58_9VIBR Unreviewed; 486 AA.
AC F9TB58;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 71.
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 ORFNames=IX91_18770 {ECO:0000313|EMBL:AIW16142.1};
OS Vibrio tubiashii ATCC 19109.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio; Vibrio oreintalis group.
OX NCBI_TaxID=1051646 {ECO:0000313|EMBL:AIW16142.1, ECO:0000313|Proteomes:UP000030071};
RN [1] {ECO:0000313|EMBL:AIW16142.1, ECO:0000313|Proteomes:UP000030071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19109 {ECO:0000313|EMBL:AIW16142.1,
RC ECO:0000313|Proteomes:UP000030071};
RA Richards G.P., Needleman D.S., Watson M.A., Bono J.L.;
RT "First Complete Genome Sequence of the Shellfish Pathogen Vibrio
RT tubiashii.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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; CP009355; AIW16142.1; -; Genomic_DNA.
DR RefSeq; WP_004747573.1; NZ_CP009355.1.
DR AlphaFoldDB; F9TB58; -.
DR STRING; 1051646.IX91_18770; -.
DR KEGG; vtu:IX91_18770; -.
DR PATRIC; fig|1051646.9.peg.3671; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_0_6; -.
DR UniPathway; UPA00529; UER00386.
DR Proteomes; UP000030071; Chromosome 2.
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; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR011264; BADH.
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; 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}.
FT DOMAIN 17..474
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 159
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT ACT_SITE 247
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 247
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT ACT_SITE 281
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT ACT_SITE 459
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 23
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 90
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 147..149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 173..176
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 241
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 249
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 281
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 382
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 452
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT BINDING 455
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
FT MOD_RES 281
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804"
SQ SEQUENCE 486 AA; 52446 MW; 487BF5E47E3EB2E8 CRC64;
MEMKSLFIDG KACHATSNEA FTTYNPANGE PLAKVGQASE QDLALAIDAA KSGFKVWSAM
SPTERSRILL KAVALLRERN DELAALEVAD TGKPLQEAIA VDIETGADVI EYFAGLAPAM
QGEQQPLSGT QFFYTRREPL GICAGIGAWN YPIQIAMWKS APALAAGNAM IFKPSEETPL
SALKLAEIFT EAGLPDGVFN VLQGDHRVGQ MLTAHPDIAK VSFTGESGTG KLVMADSAKT
LKQVTMELGG KSPMIVFDDA KLDDAVAAAM VANFYTQGEV CTHGTRVFVH ESLHDEFVAQ
LKTRTEKLIV GNPMEMETQI GALISREHLS KVLSAIESAK ASKATLLTGG YQVKENGLDK
GNFVAPTVFI DCDDDMEHVK GEIFGPVMSV LKFSQESEVI QRANNTDYGL AAGVFTQNLS
RAHRVIHQLQ AGICWVNTWG DSPAEMPVGG YKHSGIGREN GPETLRHYTQ TKSVLIELGG
YESPYE
//
