Aspartate-semialdehyde dehydrogenase - Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)

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Q8TVK0 (Q8TVK0_METKA) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 73. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Recommended name:
Aspartate-semialdehyde dehydrogenase HAMAP-Rule MF_02121
Short name=ASA dehydrogenase HAMAP-Rule MF_02121
Short name=ASADH HAMAP-Rule MF_02121
EC=1.2.1.11 HAMAP-Rule MF_02121

Alternative name(s):
Aspartate-beta-semialdehyde dehydrogenase HAMAP-Rule MF_02121

Gene names

Name:	asd HAMAP-Rule MF_02121 EMBL AAM02602.1
Ordered Locus Names:	MK1389

Organism

Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) [Reference proteome] [HAMAP]

Taxonomic identifier

190192 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanopyri › Methanopyrales › Methanopyraceae › Methanopyrus ›

Protein attributes

Sequence length	354 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate By similarity. HAMAP-Rule MF_02121
Catalytic activity	L-aspartate 4-semialdehyde + phosphate + NADP⁺ = L-4-aspartyl phosphate + NADPH. RuleBase RU004501 HAMAP-Rule MF_02121
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. RuleBase RU004502 HAMAP-Rule MF_02121 Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. RuleBase RU004502 HAMAP-Rule MF_02121 Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. RuleBase RU004502 HAMAP-Rule MF_02121
Subunit structure	Homodimer By similarity. HAMAP-Rule MF_02121
Sequence similarities	Belongs to the aspartate-semialdehyde dehydrogenase family. RuleBase RU004041 HAMAP-Rule MF_02121

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Diaminopimelate biosynthesis HAMAP-Rule MF_02121 Lysine biosynthesis HAMAP-Rule MF_02121 Methionine biosynthesis HAMAP-Rule MF_02121 Threonine biosynthesis HAMAP-Rule MF_02121
Ligand	NADP RuleBase RU004501 HAMAP-Rule MF_02121
Molecular function	Oxidoreductase RuleBase RU004501 HAMAP-Rule MF_02121
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' L-methionine biosynthetic process Inferred from electronic annotation. Source: HAMAP aspartate metabolic process Inferred from electronic annotation. Source: InterPro diaminopimelate biosynthetic process Inferred from electronic annotation. Source: HAMAP isoleucine biosynthetic process Inferred from electronic annotation. Source: InterPro lysine biosynthetic process via diaminopimelate Inferred from electronic annotation. Source: HAMAP threonine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular_function	N-acetyl-gamma-glutamyl-phosphate reductase activity Inferred from electronic annotation. Source: InterPro NAD binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: HAMAP aspartate-semialdehyde dehydrogenase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Nucleotide binding

12 – 15

NADP By similarity HAMAP-Rule MF_02121

Nucleotide binding

39 – 40

NADP By similarity HAMAP-Rule MF_02121

Nucleotide binding

183 – 184

NADP By similarity HAMAP-Rule MF_02121

Sites

Active site

153

Acyl-thioester intermediate By similarity HAMAP-Rule MF_02121 PIRSR PIRSR000148-1

Active site

246

Proton acceptor By similarity HAMAP-Rule MF_02121 PIRSR PIRSR000148-1

Binding site

114

Phosphate By similarity HAMAP-Rule MF_02121

Binding site

180

Substrate By similarity HAMAP-Rule MF_02121

Binding site

206

Substrate By similarity HAMAP-Rule MF_02121

Binding site

209

Phosphate By similarity HAMAP-Rule MF_02121

Binding site

239

Substrate By similarity HAMAP-Rule MF_02121

Sequences

Sequence

Length

Mass (Da)

Tools

Q8TVK0 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: FC680FD617562075
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FASTA

354

38,304

        10         20         30         40         50         60 
MAKVRVGVLG ATGIVGQRFI SLLADHPWFE LEAVTASPRS AGKTYAEAAK WYLEEPMPED 

        70         80         90        100        110        120 
VAELTVLETD PKEVEREADV DLVFSALPSD VARDVEPAFA EAGFAVASNA SAYRMEEDVP 

       130        140        150        160        170        180 
LVVPEVNPDH LGLIDVQRDE RDWDGFIVTN PNCSTIQMVL TLKPLMDEYG IESVVVSTMQ 

       190        200        210        220        230        240 
AVSGAGYAGV PSMAIIDNVI PYIEGEEEKM ETETLKILGE LDGDRVEFAD VKVSASCHRV 

       250        260        270        280        290        300 
PVLDGHTEAI FVATEKEADP EEAAEVLAGF RGVPQEKGLP SAPERPVVVR EEEDRPQPRF 

       310        320        330        340        350 
DRDVDGGMAV VVGRIRKDPV FGGLKYVCVG HNAVRGAAGA SVLNAELLVE EGYL

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References

[1]

"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens."
Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A.
Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE009439 Genomic DNA. Translation: AAM02602.1.
RefSeq	NP_614672.1. NC_003551.1.
3D structure databases
ProteinModelPortal	Q8TVK0.
SMR	Q8TVK0. Positions 3-351.
ModBase	Search...
Protein-protein interaction databases
STRING	190192.MK1389.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM02602; AAM02602; MK1389.
GeneID	1477984.
KEGG	mka:MK1389.
Phylogenomic databases
eggNOG	COG0136.
HOGENOM	HOG000013358.
KO	K00133.
OMA	VIDGHTE.
ProtClustDB	PRK08664.
Enzyme and pathway databases
UniPathway	UPA00034; UER00016. UPA00050; UER00463. UPA00051; UER00464.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
HAMAP	MF_02121. ASADH.
InterPro	IPR000319. Asp-semialdehyde_DH_CS. IPR005676. Asp_semi-ald_DH_pep-lack. IPR012080. Asp_semialdehyde_DH. IPR016040. NAD(P)-bd_dom. IPR000534. Semialdehyde_DH_NAD-bd. IPR012280. Semialdhyde_DH_dimer_dom. [Graphical view]
Pfam	PF01118. Semialdhyde_dh. 1 hit. PF02774. Semialdhyde_dhC. 1 hit. [Graphical view]
PIRSF	PIRSF000148. ASA_dh. 1 hit.
SMART	SM00859. Semialdhyde_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR00978. asd_EA. 1 hit.
PROSITE	PS01103. ASD. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q8TVK0_METKA

Accession

Primary (citable) accession number: Q8TVK0

Entry history

Integrated into UniProtKB/TrEMBL:	June 1, 2002
Last sequence update:	June 1, 2002
Last modified:	May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information