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CBIA_PELPD
ID   CBIA_PELPD              Reviewed;         463 AA.
AC   A1AT17;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Cobyrinate a,c-diamide synthase {ECO:0000255|HAMAP-Rule:MF_00027};
DE            EC=6.3.5.11 {ECO:0000255|HAMAP-Rule:MF_00027};
DE   AltName: Full=Cobyrinic acid a,c-diamide synthetase {ECO:0000255|HAMAP-Rule:MF_00027};
GN   Name=cbiA {ECO:0000255|HAMAP-Rule:MF_00027}; OrderedLocusNames=Ppro_2890;
OS   Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Desulfuromonadaceae; Pelobacter.
OX   NCBI_TaxID=338966;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2379 / NBRC 103807 / OttBd1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ATP-dependent amidation of the two carboxylate
CC       groups at positions a and c of cobyrinate, using either L-glutamine or
CC       ammonia as the nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00027}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP +
CC         cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate;
CC         Xref=Rhea:RHEA:26289, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:58537, ChEBI:CHEBI:58894,
CC         ChEBI:CHEBI:456216; EC=6.3.5.11; 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 sirohydrochlorin (anaerobic route):
CC       step 10/10. {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 cobyrinate and catalyzes the ultimate
CC       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 cobyrinate are activated for
CC       nucleophilic attack via formation of a phosphorylated intermediate by
CC       ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then
CC       that of the a-carboxylate. {ECO:0000255|HAMAP-Rule:MF_00027}.
CC   -!- SIMILARITY: Belongs to the CobB/CbiA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00027}.
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DR   EMBL; CP000482; ABL00488.1; -; Genomic_DNA.
DR   RefSeq; WP_011736723.1; NC_008609.1.
DR   AlphaFoldDB; A1AT17; -.
DR   SMR; A1AT17; -.
DR   STRING; 338966.Ppro_2890; -.
DR   EnsemblBacteria; ABL00488; ABL00488; Ppro_2890.
DR   KEGG; ppd:Ppro_2890; -.
DR   eggNOG; COG1797; Bacteria.
DR   HOGENOM; CLU_022752_2_0_7; -.
DR   OMA; QPFKCGP; -.
DR   OrthoDB; 692368at2; -.
DR   UniPathway; UPA00148; UER00231.
DR   Proteomes; UP000006732; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042242; F:cobyrinic acid a,c-diamide synthase 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; -; 2.
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   3: Inferred from homology;
KW   ATP-binding; Cobalamin biosynthesis; Glutamine amidotransferase; Ligase;
KW   Magnesium; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..463
FT                   /note="Cobyrinate a,c-diamide synthase"
FT                   /id="PRO_1000074393"
FT   DOMAIN          250..445
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00027"
FT   ACT_SITE        333
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00027"
FT   SITE            437
FT                   /note="Increases nucleophilicity of active site Cys"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00027"
SQ   SEQUENCE   463 AA;  48879 MW;  7843322AFFDD76FC CRC64;
     MSINGFLIAA PQSGSGKTTI SLAIMAALRR RGLVVAPFKC GPDFIDPGYH RMASGRASIN
     LDGWMCPESF VAETFRLHAE AADVAVIEAV MGLFDGLGAS PLQGSSAQIA AICGAPVVLV
     VNARGMAASA AALVKGFAEF DPDVRLAGVI FNNVGSAGHA ELLARVMASA LPEIALLGCI
     PRDEALAIPS RHLGLVTAED NPLPPEYLDR LADLAEKHLD LAGLAGLRIT PRSVGASLSR
     TNGGGMLPVR IAVARDAAFC FVYQDNLRLL REAGGELLFF SPLADGALPE GISGIYLPGG
     YPELYAERLA VNVPMLDAIR GAARDGMPLY AECGGFIYLT RGMEDSQGAP LADFAGIFPV
     RARMLPKRKA LGYRQVECLS VSILGPAGET ARGHEFHYSE ICEMPVDVTR TYSVTRQGAF
     LGQEGYCLSN CLASYVHLHF GSNPCLAPSL VAACRKFAAT RRS
 
 
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