ID   CBIA_DEHMC              Reviewed;         463 AA.
AC   Q3ZWJ9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Cobyrinate a,c-diamide synthase {ECO:0000250|UniProtKB:P29946};
DE            EC=6.3.5.11 {ECO:0000250|UniProtKB:P29946};
DE   AltName: Full=Cobyrinic acid a,c-diamide synthetase {ECO:0000250|UniProtKB:P29946};
GN   Name=cbiA; Synonyms=cobB {ECO:0000312|EMBL:CAI82403.1};
GN   OrderedLocusNames=cbdbA149;
OS   Dehalococcoides mccartyi (strain CBDB1).
OC   Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=255470;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBDB1;
RX   PubMed=16116419; DOI=10.1038/nbt1131;
RA   Kube M., Beck A., Zinder S.H., Kuhl H., Reinhardt R., Adrian L.;
RT   "Genome sequence of the chlorinated compound-respiring bacterium
RT   Dehalococcoides species strain CBDB1.";
RL   Nat. Biotechnol. 23:1269-1273(2005).
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:0000250|UniProtKB:P29946}.
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;
CC         Evidence={ECO:0000250|UniProtKB:P29946};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P29946};
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:0000250|UniProtKB:P29946}.
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:0000250|UniProtKB:P29946}.
CC   -!- SIMILARITY: Belongs to the CobB/CbiA family. {ECO:0000305}.
CC   -!- CAUTION: The physiological significance of this enzyme is not known
CC       since D.mccartyi is cobalamin auxotroph. {ECO:0000305}.
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DR   EMBL; AJ965256; CAI82403.1; -; Genomic_DNA.
DR   RefSeq; WP_011308761.1; NC_007356.1.
DR   AlphaFoldDB; Q3ZWJ9; -.
DR   KEGG; deh:cbdbA149; -.
DR   HOGENOM; CLU_022752_2_0_0; -.
DR   OMA; QPFKCGP; -.
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; Glutamine amidotransferase; Ligase; Magnesium;
KW   Nucleotide-binding.
FT   CHAIN           1..463
FT                   /note="Cobyrinate a,c-diamide synthase"
FT                   /id="PRO_1000002291"
FT   DOMAIN          252..448
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00606"
FT   ACT_SITE        335
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P29946"
FT   SITE            440
FT                   /note="Increases nucleophilicity of active site Cys"
FT                   /evidence="ECO:0000250|UniProtKB:P29946"
SQ   SEQUENCE   463 AA;  50361 MW;  E8FD6EBD46492544 CRC64;
     MNFPRIVIAG VSSSSGKTTI SSGLTAALAQ RGHKVAAYKC GPDYIDPGYL TLASNNPCHN
     LDSWMLSKDA MTEVFFHGLK NRDIALVEGV MGLYDGYSGE RPGGSTAEIA RLLSAPVILL
     VNISHMAESA AAIVLGYKNL DPRINIAGVI LNQAGSTRHY EICRKAIEKY ASTPVIGYLL
     RNKDLVIPER HLGLKTTSEG GELETFIQNL ATRIESTIDI DRILEIARNA PPLPEKPLPC
     LFPETPACPV TRIAVAKDEA FSFYYQANLD MLSDWGAELC YFSPVHDTCL PPDIGGIYIG
     GGFPEIMAAE LSANQPMKDT LTKAAADGMP IYAECGGLMY LSEAIEDFDS TKYLMLGLLP
     GISVMQKKLH RLGYTRAAVQ NDNILSAKGT ELRGHIFHWS KLPSPQTKPA YTLLEPAEFV
     GQNEGFIIGG STNVLASYLH LHFGTNPDLA KNFIRISKDF CTI