2WM1

The crystal structure of human alpha-amino-beta-carboxymuconate- epsilon-semialdehyde decarboxylase in complex with 1,3- dihydroxyacetonephosphate suggests a regulatory link between NAD synthesis and glycolysis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001760	molecular_function	aminocarboxymuconate-semialdehyde decarboxylase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006569	biological_process	L-tryptophan catabolic process
A	0008270	molecular_function	zinc ion binding
A	0016787	molecular_function	hydrolase activity
A	0016829	molecular_function	lyase activity
A	0016831	molecular_function	carboxy-lyase activity
A	0019748	biological_process	secondary metabolic process
A	0046872	molecular_function	metal ion binding
A	1904985	biological_process	negative regulation of quinolinate biosynthetic process
A	1905004	biological_process	picolinic acid biosynthetic process
A	1905012	biological_process	regulation of 'de novo' NAD biosynthetic process from L-tryptophan

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 1333

Chain	Residue
A	HIS6
A	HIS8
A	HIS174
A	ASP291
A	HOH2215

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site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 13P A 1334

Chain	Residue
A	ASP291
A	PHE294
A	LEU296
A	HOH2127
A	HOH2215
A	HOH2216
A	ARG47
A	PRO77
A	HIS174
A	TRP191

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site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 1335

Chain	Residue
A	VAL147
A	ASN148
A	GLU149
A	HOH2095

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19843166","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19843166","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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