Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C1.7: P-type atpase like

  ⌊ FunctionalDomain p-type atpase (ID 304496)

Superfamily Assignment Evidence Code(s) ISS
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Loxodonta africana Taxon ID: 9785 344294348 XP_003418880.1 (RefSeq) URP

Sequence

Length of Enzyme (full-length): 1000 | Length of Functional Domain: 407

1       10        20        30        40        50        60

MEAAHSKTTEECLAYFGVSETTGLTPDQVKRHLEKYGHNELPAEEGKSLWELVIEQFEDL
LVRILLLAACISFVLAWFEEGEETVTAFVEPFVILLILIANAIVGVWQERNAENAIEALK
EYEPEMGKVYRADRKAVQRIKARDIVPGDIVEVAVGDKVPADIRILSIKSTTLRVDQSIL
TGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKALGIVASTGVNTEIGKIRDQMA
ATEQDKTPLQQKLDEFGEQLSKVISLICVAVWLINIGHFSDPVHGGSWIRGAIYYFKIAV
ALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQ
MSVCKMFIVDKIDGDFCALNEFSITGSTYAPEGEILKNDKPVRAGQYDGLVELATICALC
NDSSLDFNETKGIYEKVGEATETALTTLVEKMNVFNTDVRSLSKVERANACNSVIRQLMK
KEFTLEFSRDRKSMSVYCSPAKSRAAVGNKMFVKGAPEGVIDRCNYVRVGTTRVPMTGPV
KEKILSVIKEWGTGRDTLRCLALATRDTPPKREDMFLEDSAKFIEYEVDLTFVGVVGMLD
PPRKEVTGSIQLCRDAGIRVIMITGDNKGTAIAICRRIGIFGENEEVAERAYTGREFDDL
PLPEQREACRRACCFARVEPTHKSKIVEYLQSYDEITAMTGDGVNDAPALKKAEIGIAMG
SGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAAL
GLPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMDRPPRTPKEPLISGWLFFRYMAIG
GYVGAATVGAAAWWFMYAEDGPHVTYSQLTHFMKCTEDNAHFEGVDCEVFEASEPMTMAL
SVLVTIEMCNALNSLSENQSLIRMPPWVNIWLVGSIGLSMSLHFLILYIDPLPMIFKLQA
LTVNQWLMVLKISLPVIGLDEILKFIARNYLEDPEDERRK
This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues
Superfamily CAR This EFD conserves 2/2 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
351 Asp (D) side chain nucleophile: forms covalent intermediate covalent catalysis -- reactant ISS
624 Thr (T) side chain interacts with substrate/intermediate substrate binding -- binding ISS
Subgroup CAR This EFD conserves 9/9 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
351 Asp (D) side chain nucleophile: attacks gamma phosphate moiety of ATP to form covalent intermediate, Mg2+ ligand covalent catalysis -- reactant,
metal ligand -- binding 		IDA PubMed:131039
352 Lys (K) side chain probable role in phosphate transfer from ATP covalent catalysis -- reactant IDA PubMed:2966962
353 Thr (T) side chain conserved in all p-type atpases -- ISS PubMed:9419228
354 Gly (G) side chain conserved in all p-type atpases -- ISS PubMed:9419228
355 Thr (T) side chain conserved in all p-type atpases -- ISS PubMed:9419228
624 Thr (T) side chain coordinates with phosphate oxygen from ATP substrate binding -- binding ISS PubMed:10191250
683 Lys (K) side chain stabilizes transition state of phosphoryl transfer by contacting beta & gamma phosphate oxygens of ATP electrostatic stabiliser -- spectator IDA PubMed:1831454
702 Asp (D) side chain Mg2+ ligand metal ligand -- binding ISS PubMed:10191250
706 Asp (D) side chain Mg2+ ligand metal ligand -- binding ISS PubMed:10191250

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
3TLM Crystal Structure Of Endoplasmic Reticulum Ca2+-Atpase (Serca) From Bovine Muscle Sarcoplasmic/Endoplasmic Reticulum Calcium Atpase 1 40 2.95 Calcium Ion
(3 more ⇓) 		CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via UniProtKB.

Curation History
Time Change Annotation Old Value New Value
Aug. 1, 2014, 1:40 p.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.