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P44336 (SERC_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoserine aminotransferase
EC=2.6.1.52
Alternative name(s):
Phosphohydroxythreonine aminotransferase
Short name=PSAT
Gene names
Name:serC
Ordered Locus Names:HI_1167
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus ›

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine By similarity. HAMAP-Rule MF_00160

Catalytic activity

O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate. HAMAP-Rule MF_00160

4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate. HAMAP-Rule MF_00160

Cofactor

Binds 1 pyridoxal phosphate per subunit By similarity.

Pathway

Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3. HAMAP-Rule MF_00160

Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5. HAMAP-Rule MF_00160

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 362362Phosphoserine aminotransferase HAMAP-Rule MF_00160
PRO_0000150174

Regions

Region76 – 772Pyridoxal phosphate binding By similarity
Region237 – 2382Pyridoxal phosphate binding By similarity

Sites

Binding site421L-glutamate By similarity
Binding site1021Pyridoxal phosphate By similarity
Binding site1521Pyridoxal phosphate By similarity
Binding site1721Pyridoxal phosphate By similarity
Binding site1951Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue1961N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P44336 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 1DBDC9F25B76C3F7

FASTA36240,313
        10         20         30         40         50         60 
MSQVFNFSAG PAMIFPEVLQ KAQNELINWL NQGVSVMEVS HRGKYFMELV TQAEKDLREV 

        70         80         90        100        110        120 
YNIPDNYRTL FLQGGARGQF ATIPMNLIGK KGKALYLNSG HWSATAAKEA RNFAEIDEIT 

       130        140        150        160        170        180 
IVENGEQTRI TDLDFSHIAD QYDYVHYCPN ETISGVEIFD VPNVGNAVLV ADMSSNILSR 

       190        200        210        220        230        240 
QIDISKFGVI YAGAQKNLGP AGITLVIIRD DLIGNARKET PSIWNYATQR DADSMINTPP 

       250        260        270        280        290        300 
TFAWYLCSLV FKHLKEIGGL EIIEKRNALK AQTLYDYIDS SKLYRNVVAK ENRSTMNVTF 

       310        320        330        340        350        360 
ITGNPELDAK FVAESTAAGL QALKGHKVLG GMRASIYNAM SQNGVEALIS FMKKFETENL 


PQ

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L42023 Genomic DNA. Translation: AAC22822.1.
PIRE64187.
RefSeqNP_439325.1. NC_000907.1.

3D structure databases

ProteinModelPortalP44336.
SMRP44336. Positions 3-359.
ModBaseSearch...

Protein-protein interaction databases

STRING71421.HI1167.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC22822; AAC22822; HI_1167.
GeneID949636.
KEGGhin:HI1167.
PATRIC20191013. VBIHaeInf48452_1219.

Phylogenomic databases

eggNOGCOG1932.
KOK00831.
OMAMSIMEMS.
ProtClustDBPRK05355.

Enzyme and pathway databases

UniPathwayUPA00135; UER00197.
UPA00244; UER00311.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_00160. SerC_aminotrans_5.
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR022278. Pser_aminoTfrase.
IPR003248. Pser_aminoTfrase_subgr.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR21152:SF1. PTHR21152:SF1. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF000525. SerC. 1 hit.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01364. serC_1. 1 hit.
PROSITEPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSERC_HAEIN
AccessionPrimary (citable) accession number: P44336
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 1, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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