CBIA_DEHM1
ID CBIA_DEHM1 Reviewed; 463 AA.
AC Q3ZA71;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
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:AAW40541.1};
GN OrderedLocusNames=DET0128;
OS Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
OS (Dehalococcoides ethenogenes (strain 195)).
OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=243164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2266 / KCTC 15142 / 195;
RX PubMed=15637277; DOI=10.1126/science.1102226;
RA Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A.,
RA Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M., Kolonay J.F., Dodson R.J.,
RA Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E.,
RA Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M.,
RA Zinder S.H., Heidelberg J.F.;
RT "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT ethenogenes.";
RL Science 307:105-108(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; CP000027; AAW40541.1; -; Genomic_DNA.
DR RefSeq; WP_010935933.1; NC_002936.3.
DR AlphaFoldDB; Q3ZA71; -.
DR SMR; Q3ZA71; -.
DR STRING; 243164.DET0128; -.
DR PRIDE; Q3ZA71; -.
DR EnsemblBacteria; AAW40541; AAW40541; DET0128.
DR KEGG; det:DET0128; -.
DR PATRIC; fig|243164.10.peg.119; -.
DR eggNOG; COG1797; Bacteria.
DR HOGENOM; CLU_022752_2_0_0; -.
DR OMA; QPFKCGP; -.
DR OrthoDB; 692368at2; -.
DR Proteomes; UP000008289; 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; -; 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; Glutamine amidotransferase; Ligase; Magnesium;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..463
FT /note="Cobyrinate a,c-diamide synthase"
FT /id="PRO_1000002290"
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; 50473 MW; D692E7228C3EEADE CRC64;
MNFPRIVIAG ISSSSGKTTI SSGITAALTK RGHKVAAYKC GPDYIDPGYL TLAADNPCHN
LDSWMLGKDA MTEVFFHGLK NREIALVEGV MGLYDGYSGE RPGGSTAEIA RLLSAPVILL
LNISHMAESA AAIVLGYKNL DPRINIAGVI LNQAGSLRHY EICRKAIEKY TSTPVVGYLL
RNKELAIPER HLGLKTTSEG GELASFIQNL AAHIESTIDI DRILNIARNA PPLPERPCPY
LFPETPARPV TRIAIARDEA FSFYYQANLD MLSDWGAELC YFSPVHDTCL PENIGGIYIG
GGFPEIMAAE LSANQAMKTA LTKAAEDGMP IYAECGGLMY LSEAIEDFDN NKYLMLGLLP
GVSVMQKKLH RLGYTRAAVQ NDNILSGKGT ELRGHIFHWS KLPSPKTKPA YTLLEPAEYA
GQNEGFIIGN STNVLASYLH LHFGTNPDLA KNFIRVSKGF YAI
