2GO1

NAD-dependent formate dehydrogenase from Pseudomonas sp.101

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0008863	molecular_function	formate dehydrogenase (NAD+) activity
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	0042183	biological_process	formate catabolic process
A	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 401

Chain	Residue
A	GLY200
A	ARG201
A	ILE202
A	HOH459
A	HOH517

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Functional Information from PROSITE/UniProt

site_id	PS00065
Number of Residues	28
Details	D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. VGTVAaGRIGlavlrrlapfdvh.LHyTD

Chain	Residue	Details
A	VAL194-ASP221

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

Chain	Residue	Details
A	MET244-ASN266

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

Chain	Residue	Details
A	PHE273-ASP289

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000269|DOI:10.1134/S1063774506040146

Chain	Residue	Details
A	GLY123
A	SER147

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000269|PubMed:8114093

Chain	Residue	Details
A	ILE148
A	ILE202
A	ARG222
A	LEU257
A	ALA283
A	VAL309
A	ILE333
A	TYR381

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site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000305|PubMed:8114093

Chain	Residue	Details
A	GLY285
A	ILE333

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Catalytic Information from CSA

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

Chain	Residue	Details
A	GLN313
A	HIS332
A	ASN146
A	ARG284

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site_id	MCSA1
Number of Residues	4
Details	M-CSA 902

Chain	Residue	Details
A	SER147	electrostatic stabiliser
A	GLY285	electrostatic stabiliser
A	PRO314	modifies pKa
A	ILE333	enhance reactivity

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