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COBB_BRUME
ID   COBB_BRUME              Reviewed;         436 AA.
AC   Q8YHU1;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=BMEI0705;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AE008917; AAL51886.1; -; Genomic_DNA.
DR   PIR; AC3340; AC3340.
DR   RefSeq; WP_002964414.1; NZ_GG703780.1.
DR   AlphaFoldDB; Q8YHU1; -.
DR   SMR; Q8YHU1; -.
DR   STRING; 224914.BMEI0705; -.
DR   EnsemblBacteria; AAL51886; AAL51886; BMEI0705.
DR   GeneID; 3787893; -.
DR   GeneID; 55590965; -.
DR   KEGG; bme:BMEI0705; -.
DR   PATRIC; fig|224914.52.peg.755; -.
DR   eggNOG; COG1797; Bacteria.
DR   OMA; QPFKCGP; -.
DR   PhylomeDB; Q8YHU1; -.
DR   UniPathway; UPA00148; UER00220.
DR   Proteomes; UP000000419; Chromosome I.
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   3: Inferred from homology;
KW   ATP-binding; Cobalamin biosynthesis; Glutamine amidotransferase; Ligase;
KW   Magnesium; Nucleotide-binding.
FT   CHAIN           1..436
FT                   /note="Hydrogenobyrinate a,c-diamide synthase"
FT                   /id="PRO_0000141255"
FT   DOMAIN          244..435
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00027"
FT   ACT_SITE        327
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00027"
FT   SITE            427
FT                   /note="Increases nucleophilicity of active site Cys"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00027"
SQ   SEQUENCE   436 AA;  47034 MW;  AED85D8A1549862B CRC64;
     MKGFMIAAPA SGSGKTTVTL GLLRALKRRG EVLAPVKAGP DYIDPAYHRA ASGVDCFNLD
     PWAMRPELIS ALSSRMTESG ARVLVAEGMM GLFDGAIDGK GSSADLARLL DLPVVLVVDC
     ARQSHSIAAL VWGFSQFRKD VLIEGVILNR VGSPRHEAML RGALAPLGVP VLGALPRDPA
     LSLPERHLGL VQADEHAGLE SFLEQAADVM EAHIDMDALQ TIWLRPKRYD AMANVARLKP
     LGNRIAVARD DAFAFAYMHL FEGWRRRGAE ISFFSPLADE APKADADAIY LPGGYPELHA
     QRLAGASRFR TAIGDAAARG VTVYGECGGY MVLGKTLEDA AGVHHPMLGL LPLETSFARR
     KLHLGYRLLE PLGGLPWDMP LKAHEFHYAS IVREEKADRL FRVRDASGEN LGEAGLRVGS
     VSGSFMHVID FSGEAA
 
 
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