6WSA

Crystal structure of a betaine aldehyde dehydrogenase from Burkholderia pseudomallei without cofactor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008802	molecular_function	betaine-aldehyde dehydrogenase activity
A	0016491	molecular_function	oxidoreductase activity
A	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A	0019145	molecular_function	aminobutyraldehyde dehydrogenase activity
A	0019285	biological_process	glycine betaine biosynthetic process from choline
A	0046872	molecular_function	metal ion binding
A	0047105	molecular_function	4-trimethylammoniobutyraldehyde dehydrogenase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue SIN A 501

Chain	Residue
A	SER2
A	HOH733
A	GLY5
A	LEU6
A	ARG8
A	HIS15
A	HOH638
A	HOH652
A	HOH681
A	HOH721

---

site_id	AC2
Number of Residues	3
Details	binding site for residue EDO A 502

Chain	Residue
A	ARG140
A	GLU470
A	THR473

---

site_id	AC3
Number of Residues	5
Details	binding site for residue EDO A 503

Chain	Residue
A	GLN157
A	TRP161
A	VAL284
A	HOH610
A	HOH797

---

site_id	AC4
Number of Residues	4
Details	binding site for residue EDO A 504

Chain	Residue
A	ARG82
A	GLU194
A	EDO508
A	HOH763

---

site_id	AC5
Number of Residues	7
Details	binding site for residue EDO A 505

Chain	Residue
A	GLY209
A	GLY212
A	ALA213
A	THR232
A	VAL236
A	HOH671
A	HOH731

---

site_id	AC6
Number of Residues	4
Details	binding site for residue EDO A 506

Chain	Residue
A	PHE279
A	GLY444
A	VAL488
A	HOH855

---

site_id	AC7
Number of Residues	3
Details	binding site for residue EDO A 507

Chain	Residue
A	ARG58
A	GLU59
A	HOH942

---

site_id	AC8
Number of Residues	6
Details	binding site for residue EDO A 508

Chain	Residue
A	SER2
A	LEU34
A	EDO504
A	HOH837
A	HOH890
A	HOH948

---

site_id	AC9
Number of Residues	5
Details	binding site for residue EDO A 509

Chain	Residue
A	LEU79
A	ARG80
A	ASN83
A	ILE106
A	VAL107

---

site_id	AD1
Number of Residues	5
Details	binding site for residue EDO A 510

Chain	Residue
A	ASP47
A	ALA51
A	HIS218
A	HOH619
A	HOH870

---

site_id	AD2
Number of Residues	4
Details	binding site for residue EDO A 511

Chain	Residue
A	ASP262
A	GLN294
A	GLN295
A	ALA296

---

site_id	AD3
Number of Residues	3
Details	binding site for residue EDO A 512

Chain	Residue
A	ASP267
A	ARG304
A	ARG308

---

site_id	AD4
Number of Residues	4
Details	binding site for residue EDO A 513

Chain	Residue
A	LEU337
A	ASP341
A	GLY354
A	HOH608

---

site_id	AD5
Number of Residues	3
Details	binding site for residue EDO A 514

Chain	Residue
A	ALA222
A	ARG474
A	HOH655

---

site_id	AD6
Number of Residues	6
Details	binding site for residue NA A 515

Chain	Residue
A	THR26
A	PHE27
A	ASP93
A	VAL180
A	HOH726
A	HOH874

---

Functional Information from PROSITE/UniProt

site_id	PS00070
Number of Residues	12
Details	ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfSAGQVCTNGT

Chain	Residue	Details
A	PHE278-THR289

---

site_id	PS00687
Number of Residues	8
Details	ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. MELGGKSP

Chain	Residue	Details
A	MET250-PRO257

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Charge relay system => ECO:0000255|HAMAP-Rule:MF_00804

Chain	Residue	Details
A	LYS162
A	GLU463

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00804

Chain	Residue	Details
A	GLU251

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00804

Chain	Residue	Details
A	CYS285

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00804

Chain	Residue	Details
A	ASP93
A	VAL180
A	LEU245
A	LYS456
A	GLY459
A	THR26

---

site_id	SWS_FT_FI5
Number of Residues	5
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00804, ECO:0007744|PDB:6WSB

Chain	Residue	Details
A	GLY229
A	GLY253
A	GLU386
A	GLY150
A	LYS176

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	BINDING: covalent => ECO:0000255|HAMAP-Rule:MF_00804, ECO:0007744|PDB:6WSB

Chain	Residue	Details
A	CYS285

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	SITE: Seems to be a necessary countercharge to the potassium cations => ECO:0000255|HAMAP-Rule:MF_00804

Chain	Residue	Details
A	GLU247

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000255|HAMAP-Rule:MF_00804

Chain	Residue	Details
A	CYS285

---