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COBQ_METVO
ID   COBQ_METVO              Reviewed;         229 AA.
AC   P21157;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Probable cobyric acid synthase;
DE   Flags: Fragment;
GN   Name=cobQ;
OS   Methanococcus voltae.
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=2188;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS;
RX   PubMed=2575777; DOI=10.1016/0923-2508(89)90012-0;
RA   Possot O., Sibold L., Aubert J.-P.;
RT   "Nucleotide sequence and expression of the glutamine synthetase structural
RT   gene, glnA, of the archaebacterium Methanococcus voltae.";
RL   Res. Microbiol. 140:355-371(1989).
RN   [2]
RP   SIMILARITY.
RX   PubMed=7899076; DOI=10.1093/nar/23.4.565;
RA   Ouzounis C., Kyrpides N., Sander C.;
RT   "Novel protein families in archaean genomes.";
RL   Nucleic Acids Res. 23:565-570(1995).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC   -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X53509; CAA37586.1; -; Genomic_DNA.
DR   PIR; B43995; B43995.
DR   AlphaFoldDB; P21157; -.
DR   SMR; P21157; -.
DR   UniPathway; UPA00148; -.
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   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00028; CobQ; 1.
DR   InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR   InterPro; IPR004459; CobQ_synth.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR21343:SF1; PTHR21343:SF1; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00313; cobQ; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Glutamine amidotransferase.
FT   CHAIN           1..>229
FT                   /note="Probable cobyric acid synthase"
FT                   /id="PRO_0000141353"
FT   NON_TER         229
SQ   SEQUENCE   229 AA;  25400 MW;  AB3EED311752B1C5 CRC64;
     MAKFIMVAGT ASNSGKTVMV SGICRMLANK GYKVAPFKSE NMSLNSRVSV EDGEIAVAQY
     TQSVAAKVEP STHFNPVLLK PKGNFTSQVI IHGKPYKNLD YNEYRNEKDY CIEKIKESLD
     YLNKNYDYVI MEGAGSCCEI NLLEDDIANL RVAEMANADV LLVSDIDRGG VFASLYGTVE
     LLPENWRKLI KGFIINKFRG NADVLTDGFK KITELTNIDV AGLIPYDES
 
 
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