5A2D

CRYSTAL STRUCTURE OF BETAINE ALDEHYDE DEHYDROGENASE FROM SPINACH SHOWING A THIOHEMIACETAL WITH BETAINE ALDEHYDE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006081	biological_process	aldehyde metabolic process
A	0008802	molecular_function	betaine-aldehyde dehydrogenase (NAD+) 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 (NAD+) activity
A	0019285	biological_process	glycine betaine biosynthetic process from choline
A	0030955	molecular_function	potassium ion binding
A	0042803	molecular_function	protein homodimerization activity
A	0046872	molecular_function	metal ion binding
A	0047105	molecular_function	4-trimethylammoniobutyraldehyde dehydrogenase activity
A	0102244	molecular_function	3-aminopropanal dehydrogenase (NAD+) activity
A	0110095	biological_process	cellular detoxification of aldehyde
B	0006081	biological_process	aldehyde metabolic process
B	0008802	molecular_function	betaine-aldehyde dehydrogenase (NAD+) activity
B	0016491	molecular_function	oxidoreductase activity
B	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B	0019145	molecular_function	aminobutyraldehyde dehydrogenase (NAD+) activity
B	0019285	biological_process	glycine betaine biosynthetic process from choline
B	0030955	molecular_function	potassium ion binding
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding
B	0047105	molecular_function	4-trimethylammoniobutyraldehyde dehydrogenase activity
B	0102244	molecular_function	3-aminopropanal dehydrogenase (NAD+) activity
B	0110095	biological_process	cellular detoxification of aldehyde
C	0006081	biological_process	aldehyde metabolic process
C	0008802	molecular_function	betaine-aldehyde dehydrogenase (NAD+) activity
C	0016491	molecular_function	oxidoreductase activity
C	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C	0019145	molecular_function	aminobutyraldehyde dehydrogenase (NAD+) activity
C	0019285	biological_process	glycine betaine biosynthetic process from choline
C	0030955	molecular_function	potassium ion binding
C	0042803	molecular_function	protein homodimerization activity
C	0046872	molecular_function	metal ion binding
C	0047105	molecular_function	4-trimethylammoniobutyraldehyde dehydrogenase activity
C	0102244	molecular_function	3-aminopropanal dehydrogenase (NAD+) activity
C	0110095	biological_process	cellular detoxification of aldehyde
D	0006081	biological_process	aldehyde metabolic process
D	0008802	molecular_function	betaine-aldehyde dehydrogenase (NAD+) activity
D	0016491	molecular_function	oxidoreductase activity
D	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D	0019145	molecular_function	aminobutyraldehyde dehydrogenase (NAD+) activity
D	0019285	biological_process	glycine betaine biosynthetic process from choline
D	0030955	molecular_function	potassium ion binding
D	0042803	molecular_function	protein homodimerization activity
D	0046872	molecular_function	metal ion binding
D	0047105	molecular_function	4-trimethylammoniobutyraldehyde dehydrogenase activity
D	0102244	molecular_function	3-aminopropanal dehydrogenase (NAD+) activity
D	0110095	biological_process	cellular detoxification of aldehyde

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CHT A 1497

Chain	Residue
A	TYR160
A	ILE290
A	CYS291
A	SER292
A	GLN448
A	CYS450

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CHT B 1497

Chain	Residue
B	ILE290
B	SER292
B	GLN448
B	CYS450
B	TYR160
B	MET164
B	TRP167

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ETX D 1498

Chain	Residue
D	PRO157
D	ASN159
D	THR234
D	GLY235
D	SER236
D	GLY259
D	CSO291
D	GLU390
D	PHE392
D	HOH2179

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ETX A 1498

Chain	Residue
A	GLU415
A	TYR416
A	ARG461

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PG4 B 1498

Chain	Residue
A	TRP471
A	GLN474
B	GLU470
B	TRP471
B	GLN474

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE AE3 C 1497

Chain	Residue
C	GLN474
D	GLU470
D	TRP471

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K A 1499

Chain	Residue
A	ILE28
A	ASP96
A	LEU186
A	HOH2022
A	HOH2023

---

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K B 1499

Chain	Residue
B	ILE28
B	ASP96
B	LEU186
B	HOH2015
B	HOH2018

---

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K C 1498

Chain	Residue
C	VAL27
C	ILE28
C	ASP96
C	LEU186
C	HOH2037

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K D 1499

Chain	Residue
D	ILE28
D	ASP96
D	LEU186
D	HOH2019
D	HOH2088

---

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 1500

Chain	Residue
C	LYS460
D	ARG55
D	PRO226
D	ASP227
D	ASP229
D	HOH2027

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
D	PHE284-SER295
C	PHE284-SER295
A	PHE284-SER295

---

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

Chain	Residue	Details
D	LEU256-PRO263
C	LEU256-PRO263
A	LEU256-PRO263

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10007","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10008","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10007","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10008","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22345508","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22345508","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26792760","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4A0M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A2D","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	40
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22345508","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4A0M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4V37","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"22345508","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26792760","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4A0M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A2D","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22345508","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4V37","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P20000","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"Blocked amino end (Arg)"}

Chain

Residue

Details

---