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6CCI

The Crystal Structure of XOAT1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0005794cellular_componentGolgi apparatus
A0009409biological_processresponse to cold
A0009414biological_processresponse to water deprivation
A0009651biological_processresponse to salt stress
A0016020cellular_componentmembrane
A0016413molecular_functionO-acetyltransferase activity
A0016740molecular_functiontransferase activity
A0045492biological_processxylan biosynthetic process
A0045893biological_processpositive regulation of DNA-templated transcription
A0050826biological_processresponse to freezing
A1990538molecular_functionxylan O-acetyltransferase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
AMET1-LYS21

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical; Signal-anchor for type II membrane protein => ECO:0000255
ChainResidueDetails
AASN22-TYR42

site_idSWS_FT_FI3
Number of Residues444
DetailsTOPO_DOM: Lumenal => ECO:0000305
ChainResidueDetails
AASN43-SER487

site_idSWS_FT_FI4
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:32354790
ChainResidueDetails
ASER216

site_idSWS_FT_FI5
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:32354790
ChainResidueDetails
AASP462

site_idSWS_FT_FI6
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:32354790
ChainResidueDetails
AHIS465

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: O-acetylserine => ECO:0000269|PubMed:32354790
ChainResidueDetails
ASER216

site_idSWS_FT_FI8
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:32354790, ECO:0007744|PDB:6CCI
ChainResidueDetails
AASN151
AASN241
AASN255
AASN393
AASN412
AASN425

222036

PDB entries from 2024-07-03

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