Pseudomonas chlororaphis subsp. aurantiaca JD37, JM49_RS03240

Cytoplasmic
Cytoplasmic Membrane
Periplasmic
Outer Membrane
Extracellular
Unknown

Gene Ontology

Ontology Accession Term GO Evidence Evidence Ontology (ECO) Code Reference Comments
Molecular Function GO:0051287 NAD binding
ISM
Inferred from Sequence Model
Term mapped from: InterPro:SM00859
ECO:0000259
match to InterPro signature evidence used in automatic assertion
Molecular Function GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
ISM
Inferred from Sequence Model
Term mapped from: InterPro:SM00859
ECO:0000259
match to InterPro signature evidence used in automatic assertion
Molecular Function GO:0070401 NADP+ binding
ISM
Inferred from Sequence Model
Term mapped from: InterPro:TIGR01850
ECO:0000259
match to InterPro signature evidence used in automatic assertion
Molecular Function GO:0003942 N-acetyl-gamma-glutamyl-phosphate reductase activity
ISM
Inferred from Sequence Model
Term mapped from: InterPro:TIGR01850
ECO:0000259
match to InterPro signature evidence used in automatic assertion
Biological Process GO:0006526 arginine biosynthetic process
ISM
Inferred from Sequence Model
Term mapped from: InterPro:TIGR01850
ECO:0000259
match to InterPro signature evidence used in automatic assertion
Molecular Function GO:0046983 protein dimerization activity
ISM
Inferred from Sequence Model
Term mapped from: InterPro:PF02774
ECO:0000259
match to InterPro signature evidence used in automatic assertion
Biological Process GO:0008652 cellular amino acid biosynthetic process
ISM
Inferred from Sequence Model
Term mapped from: InterPro:PF02774
ECO:0000259
match to InterPro signature evidence used in automatic assertion

Functional Classifications Manually Assigned by PseudoCAP

Pathways

Database Xref Pathway Version Evidence PMID
KEGG pcp00220 Arginine biosynthesis 81.0+/01-23, Jan 17 ECO:0000249
sequence similarity evidence used in automatic assertion
KEGG pcp01130 Biosynthesis of antibiotics 81.0+/01-23, Jan 17 ECO:0000249
sequence similarity evidence used in automatic assertion
KEGG pcp01210 2-Oxocarboxylic acid metabolism 81.0+/01-23, Jan 17 ECO:0000249
sequence similarity evidence used in automatic assertion
KEGG pcp01100 Metabolic pathways 81.0+/01-23, Jan 17 ECO:0000249
sequence similarity evidence used in automatic assertion
KEGG pcp01110 Biosynthesis of secondary metabolites 81.0+/01-23, Jan 17 ECO:0000249
sequence similarity evidence used in automatic assertion
KEGG pcp01230 Biosynthesis of amino acids 81.0+/01-23, Jan 17 ECO:0000249
sequence similarity evidence used in automatic assertion

Functional Predictions from Interpro

Analysis Accession Description Interpro Accession Interpro Description Amino Acid Start Amino Acid Stop E-value
Pfam PF01118 Semialdehyde dehydrogenase, NAD binding domain IPR000534 Semialdehyde dehydrogenase, NAD-binding 3 142 5.5E-39
Hamap MF_00150 N-acetyl-gamma-glutamyl-phosphate reductase [argC]. IPR000706 N-acetyl-gamma-glutamyl-phosphate reductase, type 1 2 338 44.090557
Pfam PF02774 Semialdehyde dehydrogenase, dimerisation domain IPR012280 Semialdehyde dehydrogenase, dimerisation domain 161 315 3.2E-17
NCBIfam TIGR01850 JCVI: N-acetyl-gamma-glutamyl-phosphate reductase IPR000706 N-acetyl-gamma-glutamyl-phosphate reductase, type 1 2 344 0.0
FunFam G3DSA:3.30.360.10:FF:000014 N-acetyl-gamma-glutamyl-phosphate reductase - - 148 312 1.0E-51
Gene3D G3DSA:3.30.360.10 Dihydrodipicolinate Reductase; domain 2 - - 148 312 1.3E-127
Gene3D G3DSA:3.40.50.720 - - - 3 330 1.3E-127
SUPERFAMILY SSF51735 NAD(P)-binding Rossmann-fold domains IPR036291 NAD(P)-binding domain superfamily 2 172 2.92E-54
SMART SM00859 Semialdhyde_dh_3 IPR000534 Semialdehyde dehydrogenase, NAD-binding 3 142 2.5E-66
PANTHER PTHR32338 N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED-RELATED - - 2 344 5.0E-126
SUPERFAMILY SSF55347 Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain - - 150 312 3.79E-51

Search for additional functional domains at the NCBI CDD database website. Go to this protein's amino acid sequence and follow the link.