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Database: UniProt/TrEMBL
Entry: D9QVX4_ACEAZ
LinkDB: D9QVX4_ACEAZ
Original site: D9QVX4_ACEAZ 
ID   D9QVX4_ACEAZ            Unreviewed;       203 AA.
AC   D9QVX4;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Alpha-ribazole phosphatase {ECO:0000313|EMBL:ADL12383.1};
GN   OrderedLocusNames=Acear_0848 {ECO:0000313|EMBL:ADL12383.1};
OS   Acetohalobium arabaticum (strain ATCC 49924 / DSM 5501 / Z-7288).
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC   Acetohalobium.
OX   NCBI_TaxID=574087 {ECO:0000313|EMBL:ADL12383.1, ECO:0000313|Proteomes:UP000001661};
RN   [1] {ECO:0000313|EMBL:ADL12383.1, ECO:0000313|Proteomes:UP000001661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49924 / DSM 5501 / Z-7288
RC   {ECO:0000313|Proteomes:UP000001661};
RX   PubMed=21304692;
RA   Sikorski J., Lapidus A., Chertkov O., Lucas S., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Brambilla E.,
RA   Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA   Bruce D., Detter C., Tapia R., Goodwin L., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M.,
RA   Spring S., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Acetohalobium arabaticum type strain (Z-
RT   7288).";
RL   Stand. Genomic Sci. 3:57-65(2010).
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DR   EMBL; CP002105; ADL12383.1; -; Genomic_DNA.
DR   RefSeq; WP_013277829.1; NC_014378.1.
DR   AlphaFoldDB; D9QVX4; -.
DR   STRING; 574087.Acear_0848; -.
DR   KEGG; aar:Acear_0848; -.
DR   eggNOG; COG0406; Bacteria.
DR   HOGENOM; CLU_033323_8_4_9; -.
DR   OrthoDB; 9781415at2; -.
DR   Proteomes; UP000001661; Chromosome.
DR   GO; GO:0043755; F:alpha-ribazole phosphatase activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR001345; PG/BPGM_mutase_AS.
DR   InterPro; IPR017578; Ribazole_CobC.
DR   NCBIfam; TIGR03162; ribazole_cobC; 1.
DR   PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR   PANTHER; PTHR48100:SF1; PHOSPHOGLYCERATE MUTASE PMU1-RELATED; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   PIRSF; PIRSF000709; 6PFK_2-Ptase; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001661}.
FT   ACT_SITE        10
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        83
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         9..16
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         59
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   203 AA;  23045 MW;  AC95F5F1EF93B1C5 CRC64;
     MATEIILVRH GETLWNKESR FQGSADVKLS SDGVKQAERL AERFADFRLD MVYASDLQRA
     AKTAEIVADQ HGININTEAK LREANFGVWE GLTFEEIKER DGEKLDAWLK DPVTVQTPEG
     ENFEEVQKRA KEGLNRIKTK HEDEQVLVVA HGGTIRALLV DLLGMPLSNF WRIQQDNTAV
     NIVKFYDGDP IVSLINCTQH LRE
//
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