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CBIA_ARCFU
ID   CBIA_ARCFU              Reviewed;         458 AA.
AC   O28054;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 118.
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=AF_2229;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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; AE000782; AAB89025.1; -; Genomic_DNA.
DR   PIR; E69528; E69528.
DR   AlphaFoldDB; O28054; -.
DR   SMR; O28054; -.
DR   STRING; 224325.AF_2229; -.
DR   EnsemblBacteria; AAB89025; AAB89025; AF_2229.
DR   KEGG; afu:AF_2229; -.
DR   eggNOG; arCOG00106; Archaea.
DR   HOGENOM; CLU_022752_2_0_2; -.
DR   OMA; MYLTNSI; -.
DR   PhylomeDB; O28054; -.
DR   UniPathway; UPA00148; UER00231.
DR   Proteomes; UP000002199; 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..458
FT                   /note="Cobyrinate a,c-diamide synthase"
FT                   /id="PRO_0000141273"
FT   DOMAIN          254..445
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00027"
FT   ACT_SITE        335
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   458 AA;  51628 MW;  AE6F2E0DD5713C13 CRC64;
     MKLLPMDIPR VVIAGTSSKV GKTMISIGLM RLLVNRGYEV QPYKVGPDFI DPGFHHLATG
     RYSRNLDSFM LSRSAILETF IRNFRGADVA IIEGKTGLYD SSDAVSEKGS VAEVSKILKA
     PVVLVANVER LNRTAAAIIL GYKLFDPDVL LKGVILNRVG SERHAGKVRT AVEKLAGVRV
     LGVVPRKKVK MPYRHLGLVT AYEREDMDEL LDNIAEIVEK HVDVDKILEI AEKAPPLDSV
     FEDEKEDEEK KYVKIGVIRD QVFSFYYQDN LDELSKYAEL VFVNSLTDKR LPDVDALYIG
     GGFPEVFAEG LEKNEKLRNE IYDFCQSGNP VYAECGGLMY LGESLETSEG EFEMVGFLPL
     KTKMYERFQA QGYSVYRTLK PCIIAKRNQK IVGHEFHYSR PTLTGKADFA FRVERGFGID
     GRRDGILKEN TLGCYIHVHF LSDKSIARRF VKKAMKKK
 
 
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