Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphoserine aminotransferase

Gene

serC

Organism
Bifidobacterium longum subsp. longum (strain BBMN68)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.UniRule annotationSAAS annotation

Catalytic activityi

4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate.UniRule annotationSAAS annotation
O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate.UniRule annotationSAAS annotation

Cofactori

Protein has several cofactor binding sites:
  • pyridoxal 5'-phosphateSAAS annotationNote: Binds 1 pyridoxal phosphate per subunit.SAAS annotation
  • pyridoxal 5'-phosphateUniRule annotationNote: Binds 1 pyridoxal phosphate per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei46 – 461L-glutamateUniRule annotation
Binding sitei104 – 1041Pyridoxal phosphateUniRule annotation
Binding sitei150 – 1501Pyridoxal phosphateUniRule annotation
Binding sitei174 – 1741Pyridoxal phosphateUniRule annotation
Binding sitei197 – 1971Pyridoxal phosphateUniRule annotation

GO - Molecular functioni

  1. O-phospho-L-serine:2-oxoglutarate aminotransferase activity Source: UniProtKB-HAMAP
  2. pyridoxal phosphate binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. L-serine biosynthetic process Source: UniProtKB-HAMAP
  2. pyridoxine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

AminotransferaseUniRule annotationSAAS annotation, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Pyridoxine biosynthesisUniRule annotation, Serine biosynthesisUniRule annotationSAAS annotation

Keywords - Ligandi

Pyridoxal phosphateUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCyciBLON890402:GJ8K-1740-MONOMER.
UniPathwayiUPA00135; UER00197.
UPA00244; UER00311.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoserine aminotransferaseUniRule annotation (EC:2.6.1.52UniRule annotation)
Alternative name(s):
Phosphohydroxythreonine aminotransferaseUniRule annotation
Gene namesi
Name:serCUniRule annotationImported
Ordered Locus Names:BBMN68_1690Imported
OrganismiBifidobacterium longum subsp. longum (strain BBMN68)Imported
Taxonomic identifieri890402 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium
ProteomesiUP000006891: Chromosome

Subcellular locationi

Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei198 – 1981N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotationSAAS annotation

Structurei

3D structure databases

ProteinModelPortaliE4R3F9.
SMRiE4R3F9. Positions 5-380.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni80 – 812Pyridoxal phosphate bindingUniRule annotation
Regioni255 – 2562Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000239573.
KOiK00831.
OMAiTAFWDIA.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00160. SerC_aminotrans_5.
InterProiIPR000192. Aminotrans_V_dom.
IPR022278. Pser_aminoTfrase.
IPR006272. Pser_aminoTfrase_mycobac.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF000525. SerC. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01366. serC_3. 1 hit.

Sequencei

Sequence statusi: Complete.

E4R3F9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTITLSIPES LKPEDGRFGS GPSKIRPEQI AALDAGATTL LGTSHRQAPV
60 70 80 90 100
KQLVASIREG LREFFHLPEG YEVALGNGGA SAFWEIACAS LITRRAAFGT
110 120 130 140 150
YGSFSAKFAA SAANAPFLED PVLFPGEPGT YRLPELTEGV DTYCWAHNET
160 170 180 190 200
STGVAAPIRR VAGSREAGAL TVIDGTSAAG ALPVDISQTD VYYFSPQKAF
210 220 230 240 250
GADGGLWVAI LSPEAIDRAA GVESSAHLEG AHRWVPPFLS LTTALNNSRK
260 270 280 290 300
DQTLNTPAVA TLIMMENQIR WLNNNGGLAW ATTRCAKSAS ILYSWAERSE
310 320 330 340 350
YAAPFVVDAD ARSNAVVTID LDERVQASQV LSILRENGIV DAAGYRKLGR
360 370 380
NQLRVGVFPS VEPADVMAFT KCVDYVVEHL
Length:380
Mass (Da):40,632
Last modified:February 8, 2011 - v1
Checksum:i2539EEDE1BD38B12
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002286 Genomic DNA. Translation: ADQ02734.1.
RefSeqiYP_004001288.1. NC_014656.1.

Genome annotation databases

EnsemblBacteriaiADQ02734; ADQ02734; BBMN68_1690.
GeneIDi9958421.
KEGGiblb:BBMN68_1690.
PATRICi42583113. VBIBifLon171405_1750.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002286 Genomic DNA. Translation: ADQ02734.1.
RefSeqiYP_004001288.1. NC_014656.1.

3D structure databases

ProteinModelPortaliE4R3F9.
SMRiE4R3F9. Positions 5-380.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADQ02734; ADQ02734; BBMN68_1690.
GeneIDi9958421.
KEGGiblb:BBMN68_1690.
PATRICi42583113. VBIBifLon171405_1750.

Phylogenomic databases

HOGENOMiHOG000239573.
KOiK00831.
OMAiTAFWDIA.

Enzyme and pathway databases

UniPathwayiUPA00135; UER00197.
UPA00244; UER00311.
BioCyciBLON890402:GJ8K-1740-MONOMER.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00160. SerC_aminotrans_5.
InterProiIPR000192. Aminotrans_V_dom.
IPR022278. Pser_aminoTfrase.
IPR006272. Pser_aminoTfrase_mycobac.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF000525. SerC. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01366. serC_3. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Complete genome sequence of Bifidobacterium longum subsp. longum BBMN68, a new strain from a healthy chinese centenarian."
    Hao Y., Huang D., Guo H., Xiao M., An H., Zhao L., Zuo F., Zhang B., Hu S., Song S., Chen S., Ren F.
    J. Bacteriol. 193:787-788(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BBMN68Imported.

Entry informationi

Entry nameiE4R3F9_BIFLM
AccessioniPrimary (citable) accession number: E4R3F9
Entry historyi
Integrated into UniProtKB/TrEMBL: February 8, 2011
Last sequence update: February 8, 2011
Last modified: January 7, 2015
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.