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COBQ_PICTO
ID   COBQ_PICTO              Reviewed;         469 AA.
AC   Q6L0V5;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Probable cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=PTO0812;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
CC   -!- FUNCTION: Catalyzes amidations at positions B, D, E, and G on
CC       adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine,
CC       and one molecule of ATP is hydrogenolyzed for each amidation.
CC       {ECO:0000255|HAMAP-Rule:MF_00028}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00028}.
CC   -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00028}.
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DR   EMBL; AE017261; AAT43397.1; -; Genomic_DNA.
DR   RefSeq; WP_011177613.1; NC_005877.1.
DR   AlphaFoldDB; Q6L0V5; -.
DR   SMR; Q6L0V5; -.
DR   STRING; 263820.PTO0812; -.
DR   EnsemblBacteria; AAT43397; AAT43397; PTO0812.
DR   GeneID; 2844066; -.
DR   KEGG; pto:PTO0812; -.
DR   PATRIC; fig|263820.9.peg.848; -.
DR   eggNOG; arCOG00105; Archaea.
DR   HOGENOM; CLU_019250_2_2_2; -.
DR   OMA; EIHHGVA; -.
DR   OrthoDB; 34382at2157; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000438; Chromosome.
DR   GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01750; GATase1_CobQ; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_00028; CobQ; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR   InterPro; IPR033949; CobQ_GATase1.
DR   InterPro; IPR004459; CobQ_synth.
DR   InterPro; IPR011698; GATase_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR21343:SF1; PTHR21343:SF1; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   Pfam; PF07685; GATase_3; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00313; cobQ; 1.
DR   PROSITE; PS51274; GATASE_COBBQ; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Glutamine amidotransferase; Reference proteome.
FT   CHAIN           1..469
FT                   /note="Probable cobyric acid synthase"
FT                   /id="PRO_0000141354"
FT   DOMAIN          241..427
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        319
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        419
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   469 AA;  51658 MW;  3FBB676D36DC6F9C CRC64;
     MKMIQVLGTS SDSGKSTLAT AFCRILKDLG YRVSPFKAVN MSLNSIAIKD GSEIARAQWV
     QAMAAGAEPS AYMNPVLLKP EGHHKSQVII LGRSIGSMGI NDYYNYINKN AKIIKESIDF
     LSNKYDVIIS EGAGSPAEIN LAGRDFANIY VSSLYNTPAI LVADIDRGGV FASIYGTINL
     MQRSDLLKYY IINKMRGDQS LLYPGIERIE ELTGKKCLGI VPYIDLKLPG EDSLDYNFSG
     SGSIGIVRYP YMENYSDFDP LIFNEKAFYI KNKEDLKRCD VIILPGSKDV FHDLEYINSN
     GIADSIKRCS GEKMIIGICG GYQMLGKRIN DASGVESDGV SIPGLGLLDI ETYYNKTKTT
     GSVKYRFAEN QLKINGSGTG YEIHYGSIVK NNEMPLLITD HGPEGSVSSN GMVIGTNVHG
     ILENNEFYRY ITGEYLDYDN IIENSIETLA GIVKKSINIE GFLELLNDA
 
 
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