ID A0A091MRW8_9PASS Unreviewed; 446 AA.
AC A0A091MRW8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=2-phosphoxylose phosphatase 1 {ECO:0000256|ARBA:ARBA00040357};
DE AltName: Full=Acid phosphatase-like protein 2 {ECO:0000256|ARBA:ARBA00041499};
DE Flags: Fragment;
GN ORFNames=N310_05683 {ECO:0000313|EMBL:KFP79106.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP79106.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP79106.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP79106.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-2-O-P-Xyl]-L-seryl-[protein] + H2O = 3-O-(beta-D-GlcA-(1->3)-
CC beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:56512, Rhea:RHEA-COMP:12573, Rhea:RHEA-
CC COMP:14559, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:132093,
CC ChEBI:CHEBI:140495; Evidence={ECO:0000256|ARBA:ARBA00036311};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004323}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR EMBL; KK834608; KFP79106.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091MRW8; -.
DR Proteomes; UP000053537; Unassembled WGS sequence.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR PANTHER; PTHR11567:SF125; 2-PHOSPHOXYLOSE PHOSPHATASE 1; 1.
DR PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE 3: Inferred from homology;
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000053537};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP79106.1"
FT NON_TER 446
FT /evidence="ECO:0000313|EMBL:KFP79106.1"
SQ SEQUENCE 446 AA; 51840 MW; F425543F87E49AB6 CRC64;
VHLIPVNPVR EDGLHPKSRK RIMPDLLTEP PAIDPVYEAR VYCNIPTIAE RSMEGHAPHY
FKLVSVQVLI RHGDRYPLYA IPKTKRPDID CMLLPSRKPS HPQLEAFIKH MSKGSAAQMD
GSLSSLPRYP SHSMCEMGEL TQTGVVQHLQ NGQLLREIYI NKHKLLPSDW TAKQLYLETT
GKSRTLQSAL ALLYTFLPDF DWKKINMRHQ WSTIFCSGSC DCPMRNHYLE EEQRRQYSLR
VKNNDLEKIY VDMAKIVGIP TRQLRASNPI DSLLCYFCHN ATFPCTKTGC IGMEHFKVIK
RHQLEDERER QEKKLYFLYA LLATHPLLNQ TVNRLQRIAE GKKEEVFALY SAHDVTLSPV
LSALGITEAR FPRFAARLVF ELWQDGKRLK EHFIRILYNG ADVTFQTSFC KDHYKRSNKP
MCPLEKFVSF VKRDMFLIFN STSYYD
//