Adenosylmethionine-8-amino-7-oxononanoate aminotransferase

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Q8D003 (Q8D003_YERPE) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 77. History...

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

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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:
Adenosylmethionine-8-amino-7-oxononanoate aminotransferase HAMAP-Rule MF_00834
EC=2.6.1.62 HAMAP-Rule MF_00834

Alternative name(s):
7,8-diamino-pelargonic acid aminotransferase HAMAP-Rule MF_00834
7,8-diaminononanoate synthase HAMAP-Rule MF_00834
Diaminopelargonic acid synthase HAMAP-Rule MF_00834

Gene names

Name:	bioA HAMAP-Rule MF_00834 EMBL AAM86583.1
Ordered Locus Names:	y3032 EMBL AAM86583.1, YP_1010 EMBL AAS61261.1

Organism

Yersinia pestis [Complete proteome] [HAMAP]

Taxonomic identifier

632 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia

Protein attributes

Sequence length	426 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor By similarity. HAMAP-Rule MF_00834
Catalytic activity	S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate. HAMAP-Rule MF_00834
Cofactor	Pyridoxal phosphate By similarity. HAMAP-Rule MF_00834
Pathway	Cofactor biosynthesis; biotin biosynthesis; 7,8-diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1. HAMAP-Rule MF_00834
Subunit structure	Homodimer By similarity. HAMAP-Rule MF_00834
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00834.
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily. HAMAP-Rule MF_00834

Ontologies

Keywords
Biological process	Biotin biosynthesis HAMAP-Rule MF_00834
Cellular component	Cytoplasm HAMAP-Rule MF_00834
Ligand	Pyridoxal phosphate HAMAP-Rule MF_00834 S-adenosyl-L-methionine HAMAP-Rule MF_00834
Molecular function	Aminotransferase HAMAP-Rule MF_00834 Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	biotin biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	adenosylmethionine-8-amino-7-oxononanoate transaminase activity Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Region

112 – 113

Pyridoxal phosphate binding By similarity HAMAP-Rule MF_00834

Region

308 – 309

Pyridoxal phosphate binding By similarity HAMAP-Rule MF_00834

Sites

Binding site

Substrate By similarity HAMAP-Rule MF_00834

Binding site

144

Substrate By similarity HAMAP-Rule MF_00834

Binding site

245

Pyridoxal phosphate By similarity HAMAP-Rule MF_00834

Binding site

274

Substrate By similarity HAMAP-Rule MF_00834

Binding site

307

Substrate; via carbonyl oxygen By similarity HAMAP-Rule MF_00834

Binding site

391

Substrate By similarity HAMAP-Rule MF_00834

Site

Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM By similarity HAMAP-Rule MF_00834

Amino acid modifications

Modified residue

274

N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_00834

Sequences

Sequence

Length

Mass (Da)

Tools

Q8D003 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 9ED36823944D7462
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FASTA

426

46,661

        10         20         30         40         50         60 
MTPSDLVFDQ QHIWHPYTSM TEPLPCYPVV GAEGVELQLA DGRRLIDGMS SWWAAIHGYN 

        70         80         90        100        110        120 
HPVLNFAAHQ QLDKMSHVMF GGITHPPAVK LCRQLVAMTP PPLECVFLAD SGSVSVEVAL 

       130        140        150        160        170        180 
KMALQYWQAK GERRQRILTL RHGYHGDTFG AMSVCDPQNS MHSLYQGYLA ENLFANAPQC 

       190        200        210        220        230        240 
GFDDPWDPQD IANFVALITQ HANEIAAVIL EPVVQGAGGM RIYHPSYLRE VRALCDKHQI 

       250        260        270        280        290        300 
LLIADEIATG FGRTGKLFAC EHAQIVPDIL CLGKALTGGY LTLSATLTTR AVAETISKGD 

       310        320        330        340        350        360 
AGCFMHGPTF MANPLACAVA SANLSLLAEN SWQQQVSKIE DQLKRELLPL AQEDTVADVR 

       370        380        390        400        410        420 
VLGAIGVVEM KKPVNVARLQ RSFVEQGVWI RPFGKLIYLM PPYIISQHAL TRLTAAVAAA 


VVDRGS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of Yersinia pestis KIM." Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., Nilles M.L. , Matson J.S., Blattner F.R., Perry R.D. J. Bacteriol. 184:4601-4611(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KIM EMBL AAM86583.1 and KIM10+ / Biovar Mediaevalis.
[2]	"Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans." Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R. Yang R. DNA Res. 11:179-197(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 91001 EMBL AAS61261.1 and 91001 / Biovar Mediaevalis.
[3]	"Genetics of metabolic variations between Yersinia pestis biovars and the proposal of a new biovar, microtus." Zhou D., Tong Z., Song Y., Han Y., Pei D., Pang X., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R., Du Z., Wang J., Guo Z., Wang J., Huang P., Yang R. J. Bacteriol. 186:5147-5152(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: 91001 EMBL AAS61261.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE009952 Genomic DNA. Translation: AAM86583.1. AE017042 Genomic DNA. Translation: AAS61261.1.
RefSeq	NP_670332.1. NC_004088.1. NP_992384.1. NC_005810.1.
3D structure databases
HSSP	HSSP built from PDB template 1QJ3 based on UniProtKB P12995.
ModBase	Search...
Protein-protein interaction databases
STRING	187410.y3032.
Protocols and materials databases
DNASU	1147979.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM86583; AAM86583; y3032. AAS61261; AAS61261; YP_1010.
GeneID	1147979. 2764786.
KEGG	ypk:y3032. ypm:YP_1010.
PATRIC	18620380. VBIYerPes99487_1140.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000020209.
KO	K00833.
ProtClustDB	PRK07986.
Enzyme and pathway databases
UniPathway	UPA00078; UER00160.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 2 hits.
HAMAP	MF_00834. BioA.
InterPro	IPR005814. Aminotrans_3. IPR005815. BioA. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
PANTHER	PTHR11986. PTHR11986. 1 hit. PTHR11986:SF8. PTHR11986:SF8. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR00508. bioA. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q8D003_YERPE

Accession

Primary (citable) accession number: Q8D003
Secondary accession number(s): Q74W79

Entry history

Integrated into UniProtKB/TrEMBL:	March 1, 2003
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 77 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

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information