Reviewed, UniProtKB/Swiss-Prot P56533 (BADH_GADCA)

Names and origin

Protein names

Recommended name:
    Betaine aldehyde dehydrogenase
      Short name=BADH
    EC=1.2.1.8
Alternative name(s):
    Aldehyde dehydrogenase family 9 member A1
    EC=1.2.1.3

Gene names

Name:

aldh9A1

Organism

Gadus callarias (Baltic cod)

Taxonomic identifier

8053 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Paracanthopterygii › Gadiformes › Gadidae › Gadus

Protein attributes

Sequence length	503 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Betaine aldehyde + NAD(+) + H(2)O = betaine + NADH. An aldehyde + NAD(+) + H(2)O = an acid + NADH.
Pathway	Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1.
Subunit structure	Homotetramer.
Subcellular location	CytoplasmBy similarity.
Sequence similarities	Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aldehyde dehydrogenase (NAD) activity Inferred from electronic annotation. Source: EC betaine-aldehyde dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 503

503

Betaine aldehyde dehydrogenase

PRO_0000056532

Regions

Nucleotide binding

241 – 246

6

NAD By similarity

Sites

Active site

263

1

Proton acceptor

Active site

297

1

Nucleophile

Site

166

1

Transition state stabilizer

Secondary structure

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503

Helix Strand Turn

Details...

Helix

2 – 5

4

Helix

7 – 9

3

Turn

12 – 14

3

Beta strand

22 – 24

3

Beta strand

27 – 29

3

Beta strand

38 – 41

4

Turn

43 – 45

3

Beta strand

48 – 52

5

Helix

57 – 74

18

Helix

79 – 95

17

Helix

97 – 108

12

Helix

112 – 132

21

Helix

133 – 135

3

Beta strand

138 – 142

5

Helix

144 – 146

3

Beta strand

148 – 155

8

Beta strand

157 – 162

6

Beta strand

165 – 167

3

Helix

168 – 181

14

Beta strand

185 – 189

5

Helix

196 – 207

12

Beta strand

214 – 217

4

Helix

222 – 230

9

Beta strand

236 – 241

6

Helix

243 – 254

12

Turn

255 – 257

3

Beta strand

259 – 263

5

Beta strand

269 – 272

4

Helix

278 – 287

10

Helix

291 – 294

4

Beta strand

302 – 306

5

Helix

307 – 309

3

Helix

310 – 322

13

Helix

342 – 358

17

Beta strand

361 – 364

4

Helix

374 – 376

3

Beta strand

385 – 389

5

Helix

395 – 398

4

Beta strand

403 – 411

9

Helix

414 – 422

9

Beta strand

428 – 433

6

Helix

437 – 446

10

Beta strand

449 – 455

7

Helix

470 – 472

3

Helix

481 – 485

5

Beta strand

486 – 494

9

Sequences

	Sequence		Length	Mass (Da)
	P56533-1 [UniParc]. Last modified July 15, 1998. Version 1. Checksum: 1CB2FB92FA89E577	FASTA	503	54,368
	10 20 30 40 50 60 AQLVDSMPSA STGSVVVTDD LNYWGGRRIK SKDGATTEPV FEPATGRVLC QMVPCGAEEV 70 80 90 100 110 120 DQAVQSAQAA YLKWSKMAGI ERSRVMLEAA RIIRERRDNI AKLEVINNGK TITEAEYDID 130 140 150 160 170 180 AAWQCIEYYA GLAPTLSGQH IQLPGGAFAY TRREPLGVCA GILAWNYPFM IAAWKCAPAL 190 200 210 220 230 240 ACGNAVVFKP SPMTPVTGVI LAEIFHEAGV PVGLVNVVQG GAETGSLLCH HPNVAKVSFT 250 260 270 280 290 300 GSVPTGKKVM EMSAKTVKHV TLELGGKSPL LIFKDCELEN AVRGALMANF LTQGQVCTNG 310 320 330 340 350 360 TRVFVQREIM PQFLEEVVKR TKAIVVGDPL LTETRMGGLI SKPQLDKVLG FVAQAKKEGA 370 380 390 400 410 420 RVLCGGEPLT PSDPKLKNGY FMSPCVLDNC RDDMTCVKEE IFGPVMSVLP FDTEEEVLQR 430 440 450 460 470 480 ANNTTFGLAS GVFTRDISRA HRVAANLEAG TCYINTYSIS PVEVPFGGYK MSGFGRENGQ 490 500 ATVDYYSQLK TVIVEMGDVD SLF

References

[1]	"Structure of betaine aldehyde dehydrogenase at 2.1-A resolution." Johansson K., El-Ahmad M., Ramaswamy S., Hjelmqvist L., Joernvall H., Eklund H. Protein Sci. 7:2106-2117(1998) [PubMed: 9792097] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). Tissue: Liver.

Cross-references

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A4S	X-ray	2.10	A/B/C/D	1-503	[»]
1BPW	X-ray	2.80	A/B/C/D	1-503	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:2908N.

Phylogenomic databases

HOVERGEN

P56533.

Family and domain databases

InterPro

IPR016160. Ald_DHase_CS.
IPR016162. Ald_DHase_N.
IPR015590. Aldehyde_DHase.
[Graphical view]

Gene3D

G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.

PANTHER

PTHR11699. Aldehyde_dehyd. 1 hit.

Pfam

PF00171. Aldedh. 1 hit.
[Graphical view]

PROSITE

PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

P56533.

Entry information

Entry name

BADH_GADCA

Accession

Primary (citable) accession number: P56533

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 15, 1998
Last modified:	November 4, 2008
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)