P49420

PR
Gene name
asd
Protein name
Aspartate-semialdehyde dehydrogenase
Names
ASA dehydrogenase, ASADH, Aspartate-beta-semialdehyde dehydrogenase
Species
Prochlorococcus marinus (strain SARG / CCMP1375 / SS120)
KEGG Pathway
pma:Pro_1814
EC number
1.2.1.11: With NAD(+) or NADP(+) as acceptor
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

135-208 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P49420

Entry ID Method Resolution Chain Position Source
AF-P49420-F1 Predicted AlphaFoldDB

No variants for P49420

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P49420

No associated diseases with P49420

3 regional properties for P49420

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 113 - 432 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 16 - 94 IPR004365
domain Aminoacyl-tRNA synthetase, class II 131 - 438 IPR006195

Functions

Description
EC Number 1.2.1.11 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

4 GO annotations of molecular function

Name Definition
aspartate-semialdehyde dehydrogenase activity Catalysis of the reaction: L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH.
NAD binding Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
NADP binding Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
protein dimerization activity The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.

5 GO annotations of biological process

Name Definition
'de novo' L-methionine biosynthetic process The chemical reactions and pathways resulting in the formation of L-methionine, the L-enantiomer of (2S)-2-amino-4-(methylsulfanyl)butanoic acid, from simpler components.
diaminopimelate biosynthetic process The chemical reactions and pathways resulting in the formation of diaminopimelate, both as an intermediate in lysine biosynthesis and as a component (as meso-diaminopimelate) of the peptidoglycan of Gram-negative bacterial cell walls.
isoleucine biosynthetic process The chemical reactions and pathways resulting in the formation of isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid.
lysine biosynthetic process via diaminopimelate The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate.
threonine biosynthetic process The chemical reactions and pathways resulting in the formation of threonine (2-amino-3-hydroxybutyric acid), a polar, uncharged, essential amino acid found in peptide linkage in proteins.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTLQKPFPDR PLTLAVLGSS GAVGAEILKI LEERSFPIRE LRLLASERSA GQVQFFKGED
70 80 90 100 110 120
LVVKKVSPEG FEDVDLVLAS AGGSISRKWR KVINSAGAVI VDNSNAYRME PDVPLVVPEV
130 140 150 160 170 180
NPSQVFTHKG LIANPNCTTI LLALVLAPLS AQLPIKRVVV STYQSASGAG ARAMNELKQL
190 200 210 220 230 240
SQDVLNGNIP KSEILPYSLA FNLFLHNSPL QSNNYCEEEM KMINETRKIL NQSELAITAT
250 260 270 280 290 300
CVRVPVLRAH SESINIEFAE PFPVEEARKI LSNASGIKLL EDIQMNRFPM PIDVTGKDDI
310 320 330 340
AVGRIRQDLS NPKALELWLC GDQIRKGAAL NAIQIAELLL TRS