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Protein

Serine hydroxymethyltransferase, cytosolic

Gene

SHMT1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Interconversion of serine and glycine.1 Publication

Catalytic activityi

5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine.1 Publication

Cofactori

pyridoxal 5'-phosphate1 Publication

Pathwayi: tetrahydrofolate interconversion

This protein is involved in the pathway tetrahydrofolate interconversion, which is part of One-carbon metabolism.Curated
View all proteins of this organism that are known to be involved in the pathway tetrahydrofolate interconversion and in One-carbon metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei204Nucleophile1 Publication1
Active sitei256Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi2.1.2.1. 1749.
UniPathwayiUPA00193.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine hydroxymethyltransferase, cytosolic (EC:2.1.2.11 Publication)
Short name:
SHMT
Alternative name(s):
Glycine hydroxymethyltransferase
Serine methylase
Gene namesi
Name:SHMT1
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001135062 – 484Serine hydroxymethyltransferase, cytosolicAdd BLAST483

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Cross-linki6 ↔ 7Isoaspartyl glycine isopeptide (Asn-Gly); alternate1 Publication
Modified residuei6Deamidated asparagine; alternate1 Publication1
Modified residuei257N6-(pyridoxal phosphate)lysine1 Publication1

Post-translational modificationi

Deamidation of asparagine produces alternatively aspartate or isoaspartate, which in turn can be converted to aspartate through carboxylmethylation/demethylation.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond

Proteomic databases

PRIDEiP07511.

Interactioni

Subunit structurei

Homotetramer (PubMed:10387080). Identified in complex with FAM175B and the other subunits of the BRISC complex, at least composed of FAM175B/ABRO1, BRCC3/BRCC36, BRE/BRCC45 and BABAM1/NBA1.By similarity1 Publication

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000017814.

Structurei

Secondary structure

1484
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi18 – 21Combined sources4
Beta strandi22 – 24Combined sources3
Helixi26 – 29Combined sources4
Helixi31 – 45Combined sources15
Beta strandi46 – 49Combined sources4
Helixi59 – 65Combined sources7
Helixi68 – 70Combined sources3
Beta strandi80 – 84Combined sources5
Helixi87 – 103Combined sources17
Turni108 – 110Combined sources3
Beta strandi111 – 114Combined sources4
Helixi120 – 131Combined sources12
Beta strandi137 – 141Combined sources5
Helixi143 – 145Combined sources3
Helixi149 – 151Combined sources3
Helixi162 – 166Combined sources5
Beta strandi167 – 172Combined sources6
Turni176 – 178Combined sources3
Beta strandi179 – 181Combined sources3
Helixi183 – 193Combined sources11
Beta strandi196 – 200Combined sources5
Helixi211 – 220Combined sources10
Beta strandi224 – 228Combined sources5
Turni230 – 232Combined sources3
Helixi233 – 238Combined sources6
Helixi244 – 246Combined sources3
Beta strandi249 – 256Combined sources8
Helixi257 – 259Combined sources3
Beta strandi265 – 270Combined sources6
Helixi288 – 296Combined sources9
Turni297 – 300Combined sources4
Helixi306 – 319Combined sources14
Helixi322 – 344Combined sources23
Helixi350 – 352Combined sources3
Beta strandi355 – 362Combined sources8
Helixi363 – 366Combined sources4
Helixi370 – 379Combined sources10
Beta strandi385 – 387Combined sources3
Beta strandi395 – 397Combined sources3
Beta strandi400 – 404Combined sources5
Helixi406 – 410Combined sources5
Helixi415 – 437Combined sources23
Helixi445 – 453Combined sources9
Helixi456 – 473Combined sources18
Beta strandi480 – 482Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CJ0X-ray2.80A/B15-484[»]
1LS3X-ray2.70A/B/C/D2-484[»]
1RV3X-ray2.40A/B2-484[»]
1RV4X-ray2.95A/B2-484[»]
1RVUX-ray2.50A/B2-484[»]
1RVYX-ray2.90A/B2-484[»]
ProteinModelPortaliP07511.
SMRiP07511.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07511.

Family & Domainsi

Sequence similaritiesi

Belongs to the SHMT family.Curated

Phylogenomic databases

eggNOGiKOG2467. Eukaryota.
COG0112. LUCA.
GeneTreeiENSGT00390000002762.
HOGENOMiHOG000239405.
HOVERGENiHBG002807.
InParanoidiP07511.
KOiK00600.
OMAiDANNPAV.
OrthoDBiEOG091G05AU.
TreeFamiTF314667.

Family and domain databases

CDDicd00378. SHMT. 1 hit.
Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00051. SHMT. 1 hit.
InterProiIPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR001085. Ser_HO-MeTrfase.
IPR019798. Ser_HO-MeTrfase_PLP_BS.
[Graphical view]
PANTHERiPTHR11680. PTHR11680. 1 hit.
PfamiPF00464. SHMT. 1 hit.
[Graphical view]
PIRSFiPIRSF000412. SHMT. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00096. SHMT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07511-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATAVNGAPR DAALWSSHEQ MLAQPLKDSD AEVYDIIKKE SNRQRVGLEL
60 70 80 90 100
IASENFASRA VLEALGSCLN NKYSEGYPGQ RYYGGTEHID ELETLCQKRA
110 120 130 140 150
LQAYGLDPQC WGVNVQPYSG SPANFAVYTA LVEPHGRIMG LDLPDGGHLT
160 170 180 190 200
HGFMTDKKKI SATSIFFESM AYKVNPDTGY IDYDRLEENA RLFHPKLIIA
210 220 230 240 250
GTSCYSRNLD YGRLRKIADE NGAYLMADMA HISGLVVAGV VPSPFEHCHV
260 270 280 290 300
VTTTTHKTLR GCRAGMIFYR RGVRSVDPKT GKEILYNLES LINSAVFPGL
310 320 330 340 350
QGGPHNHAIA GVAVALKQAM TPEFKEYQRQ VVANCRALSA ALVELGYKIV
360 370 380 390 400
TGGSDNHLIL VDLRSKGTDG GRAEKVLEAC SIACNKNTCP GDKSALRPSG
410 420 430 440 450
LRLGTPALTS RGLLEKDFQK VAHFIHRGIE LTVQIQDDTG PRATLKEFKE
460 470 480
KLAGDEKHQR AVRALRQEVE SFAALFPLPG LPGF
Length:484
Mass (Da):52,975
Last modified:January 23, 2007 - v2
Checksum:iC2742A5A8052C5BF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11846 mRNA. Translation: CAA77870.1.
PIRiS24342. XYRBSC.
RefSeqiNP_001095187.1. NM_001101717.1.
UniGeneiOcu.2076.

Genome annotation databases

EnsembliENSOCUT00000030926; ENSOCUP00000017814; ENSOCUG00000021541.
GeneIDi100009405.
KEGGiocu:100009405.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11846 mRNA. Translation: CAA77870.1.
PIRiS24342. XYRBSC.
RefSeqiNP_001095187.1. NM_001101717.1.
UniGeneiOcu.2076.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CJ0X-ray2.80A/B15-484[»]
1LS3X-ray2.70A/B/C/D2-484[»]
1RV3X-ray2.40A/B2-484[»]
1RV4X-ray2.95A/B2-484[»]
1RVUX-ray2.50A/B2-484[»]
1RVYX-ray2.90A/B2-484[»]
ProteinModelPortaliP07511.
SMRiP07511.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000017814.

Proteomic databases

PRIDEiP07511.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSOCUT00000030926; ENSOCUP00000017814; ENSOCUG00000021541.
GeneIDi100009405.
KEGGiocu:100009405.

Organism-specific databases

CTDi6470.

Phylogenomic databases

eggNOGiKOG2467. Eukaryota.
COG0112. LUCA.
GeneTreeiENSGT00390000002762.
HOGENOMiHOG000239405.
HOVERGENiHBG002807.
InParanoidiP07511.
KOiK00600.
OMAiDANNPAV.
OrthoDBiEOG091G05AU.
TreeFamiTF314667.

Enzyme and pathway databases

UniPathwayiUPA00193.
BRENDAi2.1.2.1. 1749.

Miscellaneous databases

EvolutionaryTraceiP07511.

Family and domain databases

CDDicd00378. SHMT. 1 hit.
Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00051. SHMT. 1 hit.
InterProiIPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR001085. Ser_HO-MeTrfase.
IPR019798. Ser_HO-MeTrfase_PLP_BS.
[Graphical view]
PANTHERiPTHR11680. PTHR11680. 1 hit.
PfamiPF00464. SHMT. 1 hit.
[Graphical view]
PIRSFiPIRSF000412. SHMT. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00096. SHMT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGLYC_RABIT
AccessioniPrimary (citable) accession number: P07511
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

In eukaryotes there are two forms of the enzymes: a cytosolic one and a mitochondrial one.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.