2J6I

Candida boidinii formate dehydrogenase (FDH) C-terminal mutant

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006734	biological_process	NADH metabolic process
A	0006735	biological_process	NADH regeneration
A	0008863	molecular_function	formate dehydrogenase (NAD+) activity
A	0015946	biological_process	methanol oxidation
A	0016491	molecular_function	oxidoreductase activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0019752	biological_process	carboxylic acid metabolic process
A	0030416	biological_process	methylamine metabolic process
A	0042183	biological_process	formate catabolic process
A	0042426	biological_process	choline catabolic process
A	0042803	molecular_function	protein homodimerization activity
A	0051287	molecular_function	NAD binding
A	0070403	molecular_function	NAD+ binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006734	biological_process	NADH metabolic process
B	0006735	biological_process	NADH regeneration
B	0008863	molecular_function	formate dehydrogenase (NAD+) activity
B	0015946	biological_process	methanol oxidation
B	0016491	molecular_function	oxidoreductase activity
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0019752	biological_process	carboxylic acid metabolic process
B	0030416	biological_process	methylamine metabolic process
B	0042183	biological_process	formate catabolic process
B	0042426	biological_process	choline catabolic process
B	0042803	molecular_function	protein homodimerization activity
B	0051287	molecular_function	NAD binding
B	0070403	molecular_function	NAD+ binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006734	biological_process	NADH metabolic process
C	0006735	biological_process	NADH regeneration
C	0008863	molecular_function	formate dehydrogenase (NAD+) activity
C	0015946	biological_process	methanol oxidation
C	0016491	molecular_function	oxidoreductase activity
C	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0019752	biological_process	carboxylic acid metabolic process
C	0030416	biological_process	methylamine metabolic process
C	0042183	biological_process	formate catabolic process
C	0042426	biological_process	choline catabolic process
C	0042803	molecular_function	protein homodimerization activity
C	0051287	molecular_function	NAD binding
C	0070403	molecular_function	NAD+ binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006734	biological_process	NADH metabolic process
D	0006735	biological_process	NADH regeneration
D	0008863	molecular_function	formate dehydrogenase (NAD+) activity
D	0015946	biological_process	methanol oxidation
D	0016491	molecular_function	oxidoreductase activity
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0019752	biological_process	carboxylic acid metabolic process
D	0030416	biological_process	methylamine metabolic process
D	0042183	biological_process	formate catabolic process
D	0042426	biological_process	choline catabolic process
D	0042803	molecular_function	protein homodimerization activity
D	0051287	molecular_function	NAD binding
D	0070403	molecular_function	NAD+ binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PG4 A1354

Chain	Residue
A	LEU28
A	GLY29
A	TRP33
A	VAL328
A	HOH2524
A	HOH2531
A	HOH2576
A	HOH2577
C	ASP292

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PG4 C1354

Chain	Residue
C	TYR21
C	LEU28
C	GLY29
C	TRP33
C	ALA324
C	GLN325
C	VAL328

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PG4 D1354

Chain	Residue
D	TYR21
D	GLY29
D	TRP33
D	VAL328
D	HOH2458

---

Functional Information from PROSITE/UniProt

site_id	PS00065
Number of Residues	29
Details	D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. IATIGaGRIGyrvlerlvpfnpkeLLyYD

Chain	Residue	Details
A	ILE167-ASP195

---

site_id	PS00670
Number of Residues	23
Details	D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LVaqADIVtVNaPlhagTkgLiN

Chain	Residue	Details
A	LEU218-ASN240

---

site_id	PS00671
Number of Residues	17
Details	D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. FKkGaWLVNtARGaICV

Chain	Residue	Details
A	PHE247-VAL263

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	32
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03210

Chain	Residue	Details
A	VAL93
B	ASN119
B	ARG174
B	ASP195
B	PRO230
B	THR256
B	ASP282
B	HIS311
C	VAL93
C	ASN119
C	ARG174
A	ASN119
C	ASP195
C	PRO230
C	THR256
C	ASP282
C	HIS311
D	VAL93
D	ASN119
D	ARG174
D	ASP195
D	PRO230
A	ARG174
D	THR256
D	ASP282
D	HIS311
A	ASP195
A	PRO230
A	THR256
A	ASP282
A	HIS311
B	VAL93

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	SITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000305|PubMed:17525463

Chain	Residue	Details
A	ARG258
A	HIS311
B	ARG258
B	HIS311
C	ARG258
C	HIS311
D	ARG258
D	HIS311

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 2nac

Chain	Residue	Details
A	HIS311
A	GLN287
A	ASN119
A	ARG258

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 2nac

Chain	Residue	Details
B	HIS311
B	GLN287
B	ASN119
B	ARG258

---

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 2nac

Chain	Residue	Details
C	HIS311
C	GLN287
C	ASN119
C	ARG258

---

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 2nac

Chain	Residue	Details
D	HIS311
D	GLN287
D	ASN119
D	ARG258

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