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COBB_MYCTU
ID   COBB_MYCTU              Reviewed;         457 AA.
AC   P9WP97; L0TCF1; O05811; P63835;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Hydrogenobyrinate a,c-diamide synthase {ECO:0000255|HAMAP-Rule:MF_00027};
DE            EC=6.3.5.9 {ECO:0000255|HAMAP-Rule:MF_00027};
DE   AltName: Full=Hydrogenobyrinic acid a,c-diamide synthase {ECO:0000255|HAMAP-Rule:MF_00027};
GN   Name=cobB {ECO:0000255|HAMAP-Rule:MF_00027}; OrderedLocusNames=Rv2848c;
GN   ORFNames=MTCY24A1.09;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amidation of the two carboxylate
CC       groups at positions a and c of hydrogenobyrinate, using either L-
CC       glutamine or ammonia as the nitrogen source. {ECO:0000255|HAMAP-
CC       Rule:MF_00027}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + 2 H2O + hydrogenobyrinate + 2 L-glutamine = 2 ADP + 2
CC         H(+) + hydrogenobyrinate a,c-diamide + 2 L-glutamate + 2 phosphate;
CC         Xref=Rhea:RHEA:12544, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:77873, ChEBI:CHEBI:77874,
CC         ChEBI:CHEBI:456216; EC=6.3.5.9; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00027};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00027};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 9/10.
CC       {ECO:0000255|HAMAP-Rule:MF_00027}.
CC   -!- DOMAIN: Comprises of two domains. The C-terminal domain contains the
CC       binding site for glutamine and catalyzes the hydrolysis of this
CC       substrate to glutamate and ammonia. The N-terminal domain is
CC       anticipated to bind ATP and hydrogenobyrinate and catalyzes the
CC       ultimate synthesis of the diamide product. The ammonia produced via the
CC       glutaminase domain is probably translocated to the adjacent domain via
CC       a molecular tunnel, where it reacts with an activated intermediate.
CC       {ECO:0000255|HAMAP-Rule:MF_00027}.
CC   -!- MISCELLANEOUS: The a and c carboxylates of hydrogenobyrinate are
CC       activated for nucleophilic attack via formation of a phosphorylated
CC       intermediate by ATP. CobB catalyzes first the amidation of the c-
CC       carboxylate, and then that of the a-carboxylate. {ECO:0000255|HAMAP-
CC       Rule:MF_00027}.
CC   -!- SIMILARITY: Belongs to the CobB/CbiA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00027}.
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DR   EMBL; AL123456; CCP45649.1; -; Genomic_DNA.
DR   PIR; C70589; C70589.
DR   RefSeq; NP_217364.1; NC_000962.3.
DR   RefSeq; WP_003899509.1; NZ_NVQJ01000006.1.
DR   AlphaFoldDB; P9WP97; -.
DR   SMR; P9WP97; -.
DR   STRING; 83332.Rv2848c; -.
DR   PaxDb; P9WP97; -.
DR   DNASU; 888499; -.
DR   GeneID; 888499; -.
DR   KEGG; mtu:Rv2848c; -.
DR   TubercuList; Rv2848c; -.
DR   eggNOG; COG1797; Bacteria.
DR   OMA; QPFKCGP; -.
DR   PhylomeDB; P9WP97; -.
DR   UniPathway; UPA00148; UER00220.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042242; F:cobyrinic acid a,c-diamide synthase activity; IEA:InterPro.
DR   GO; GO:0043802; F:hydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_00027; CobB_CbiA; 1.
DR   InterPro; IPR004484; CbiA_synth.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR   InterPro; IPR011698; GATase_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR43873; PTHR43873; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   Pfam; PF07685; GATase_3; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00379; cobB; 1.
DR   PROSITE; PS51274; GATASE_COBBQ; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cobalamin biosynthesis; Glutamine amidotransferase; Ligase;
KW   Magnesium; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..457
FT                   /note="Hydrogenobyrinate a,c-diamide synthase"
FT                   /id="PRO_0000141262"
FT   DOMAIN          255..441
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00027"
FT   ACT_SITE        337
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00027"
FT   SITE            433
FT                   /note="Increases nucleophilicity of active site Cys"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00027"
SQ   SEQUENCE   457 AA;  46958 MW;  BD616CB55C447064 CRC64;
     MRVSAVAVAA PASGSGKTTI ATGLIGALRQ AGHTVAPFKV GPDFIDPGYH ALAAGRPGRN
     LDPVLVGERL IGPLYAHGVA GADIAVIEGV LGLFDGRIGP AGGAPAAGST AHVAALLGAP
     VILVVDARGQ SHSVAALLHG FSTFDTATRI AGVILNRVGS ARHEQVLRQA CDQAGVAVLG
     AIPRTAELEL PTRYLGLVTA VEYGRRARLA VQAMTAVVAR HVDLAAVIAC AGSQAAHPPW
     DPVIAVGNTA RQPATVAIAA GRAFTFGYAE HAEMLRAAGA EVVEFDPLSE TLPEGTDAVV
     LPGGFPEQFT AELSANDTVR RQINELAAAG APVHAECAGL LYLVSELDGH PMCGVVAGSA
     RFTQHLKLGY RDAVAVVDSA LYSVGERVVG HEFHRTAVTF ADSYQPAWVY QGQDVDDVRD
     GAVHSGVHAS YLHTHPAATP GAVARFVAHA ACNTPRA
 
 
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