3QAN

Crystal structure of 1-pyrroline-5-carboxylate dehydrogenase from bacillus halodurans

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003842	molecular_function	L-glutamate gamma-semialdehyde dehydrogenase activity
A	0004657	molecular_function	proline dehydrogenase activity
A	0006537	biological_process	obsolete glutamate biosynthetic process
A	0009898	cellular_component	cytoplasmic side of plasma membrane
A	0010133	biological_process	obsolete L-proline catabolic process to L-glutamate
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
B	0003842	molecular_function	L-glutamate gamma-semialdehyde dehydrogenase activity
B	0004657	molecular_function	proline dehydrogenase activity
B	0006537	biological_process	obsolete glutamate biosynthetic process
B	0009898	cellular_component	cytoplasmic side of plasma membrane
B	0010133	biological_process	obsolete L-proline catabolic process to L-glutamate
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
C	0003842	molecular_function	L-glutamate gamma-semialdehyde dehydrogenase activity
C	0004657	molecular_function	proline dehydrogenase activity
C	0006537	biological_process	obsolete glutamate biosynthetic process
C	0009898	cellular_component	cytoplasmic side of plasma membrane
C	0010133	biological_process	obsolete L-proline catabolic process to L-glutamate
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT C 538

Chain	Residue
C	ASN182
C	PHE183
C	LYS319
C	CYS320
C	SER321
C	PHE484

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE313-SER324

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

Chain	Residue	Details
A	VAL285-THR292

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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