Q7TUP0 (Q7TUP0_PROMM) Unreviewed, UniProtKB/TrEMBL
Last modified
January 25, 2012.
Version 63.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Alanine racemase HAMAP MF_01201 RuleBase RU000608 EC=5.1.1.1 HAMAP MF_01201 RuleBase RU000608 | ||||
| Gene names |
| ||||
| Organism | Prochlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 74547 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus |
Protein attributes
| Sequence length | 398 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Provides the D-alanine required for cell wall biosynthesis By similarity. HAMAP MF_01201 |
| Catalytic activity | L-alanine = D-alanine. HAMAP MF_01201 RuleBase RU000608 SAAS SAAS009006 |
| Cofactor | Pyridoxal phosphate By similarity. HAMAP MF_01201 RuleBase RU000608 SAAS SAAS009006 |
| Pathway | Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. HAMAP MF_01201 RuleBase RU004247 SAAS SAAS009006 Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_01201 |
| Sequence similarities | Belongs to the alanine racemase family. HAMAP MF_01201 RuleBase RU004188 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell shape Cell wall biogenesis/degradation HAMAP MF_01201 Peptidoglycan synthesis HAMAP MF_01201 |
| Ligand | Pyridoxal phosphate SAAS SAAS009006 HAMAP MF_01201 RuleBase RU000608 |
| Molecular function | Isomerase HAMAP MF_01201 RuleBase RU000608 SAAS SAAS009006 EMBL CAE21938.1 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | alanine metabolic process Inferred from electronic annotation. Source: HAMAP cellular cell wall organizationInferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic processInferred from electronic annotation. Source: HAMAP regulation of cell shapeInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | alanine racemase activity Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate bindingInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Active site | 60 | 1 | Proton acceptor; specific for D-alanine By similarity HAMAP MF_01201 | ||||||
| Active site | 291 | 1 | Proton acceptor; specific for L-alanine By similarity HAMAP MF_01201 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 60 | 1 | N6-(pyridoxal phosphate)lysine By similarity HAMAP MF_01201 | ||||||
Sequences
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References
| [1] | "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation." Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. Chisholm S.W.Nature 424:1042-1047(2003) [PubMed: 12917642] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX548175 Genomic DNA. Translation: CAE21938.1. |
| RefSeq | NP_895590.1. NC_005071.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1NIU based on UniProtKB P10724. |
| ProteinModelPortal | Q7TUP0. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q7TUP0. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1729151. |
| GenomeReviews | Gene locus PMT_1763 in contig BX548175_GR. |
| KEGG | pmt:PMT1763. |
| NMPDR | fig|74547.1.peg.1757. |
| PATRIC | 23012279. VBIProMar135351_2271. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0787. |
| HOGENOM | HBG712172. |
| OMA | TRKEDAN. |
| PhylomeDB | Q7TUP0. |
| ProtClustDB | PRK00053. |
Enzyme and pathway databases | |
| BioCyc | PMAR74547:PMT1763-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01201. Ala_racemase. [Tree] |
| InterPro | IPR000821. Ala_racemase. IPR009006. Ala_racemase/Decarboxylase_C. IPR011079. Ala_racemase_C. IPR001608. Ala_racemase_N. IPR020622. Ala_racemase_pyridoxalP-BS. [Graphical view] |
| Gene3D | G3DSA:2.40.37.10. Ala_racemase/Decarboxylase_C. 1 hit. |
| KO | K01775. |
| Pfam | PF00842. Ala_racemase_C. 1 hit. PF01168. Ala_racemase_N. 1 hit. [Graphical view] |
| PRINTS | PR00992. ALARACEMASE. |
| SMART | SM01005. Ala_racemase_C. 1 hit. [Graphical view] |
| SUPFAM | SSF50621. Racem_decarbox_C. 1 hit. |
| TIGRFAMs | TIGR00492. Alr. 1 hit. |
| PROSITE | PS00395. ALANINE_RACEMASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | Q7TUP0_PROMM | ||||||||
| Accession | Primary (citable) accession number: Q7TUP0 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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