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Entry: A0A0S4LP60_9BACT
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ID   A0A0S4LP60_9BACT        Unreviewed;       466 AA.
AC   A0A0S4LP60;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Cobyrinate a,c-diamide synthase {ECO:0000256|HAMAP-Rule:MF_00027};
DE            EC=6.3.5.11 {ECO:0000256|HAMAP-Rule:MF_00027};
DE   AltName: Full=Cobyrinic acid a,c-diamide synthetase {ECO:0000256|HAMAP-Rule:MF_00027};
GN   Name=cobB {ECO:0000313|EMBL:CUS39039.1};
GN   Synonyms=cbiA {ECO:0000256|HAMAP-Rule:MF_00027};
GN   ORFNames=COMA2_60119 {ECO:0000313|EMBL:CUS39039.1};
OS   Candidatus Nitrospira nitrificans.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Nitrospira.
OX   NCBI_TaxID=1742973 {ECO:0000313|EMBL:CUS39039.1, ECO:0000313|Proteomes:UP000198736};
RN   [1] {ECO:0000313|Proteomes:UP000198736}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Luecker S., Luecker S.;
RL   Submitted (OCT-2015) 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:0000256|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:0000256|HAMAP-
CC         Rule:MF_00027};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00027}.
CC   -!- SIMILARITY: Belongs to the CobB/CbiA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00027}.
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DR   EMBL; CZPZ01000033; CUS39039.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S4LP60; -.
DR   STRING; 1742973.COMA2_60119; -.
DR   OrthoDB; 9764035at2; -.
DR   UniPathway; UPA00148; UER00231.
DR   Proteomes; UP000198736; Unassembled WGS sequence.
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-UniRule.
DR   CDD; cd05388; CobB_N; 1.
DR   CDD; cd03130; GATase1_CobB; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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   NCBIfam; TIGR00379; cobB; 1.
DR   PANTHER; PTHR43873; COBYRINATE A,C-DIAMIDE SYNTHASE; 1.
DR   PANTHER; PTHR43873:SF1; COBYRINATE A,C-DIAMIDE SYNTHASE; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   Pfam; PF07685; GATase_3; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51274; GATASE_COBBQ; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00027}; Cobalamin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00027};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|HAMAP-Rule:MF_00027};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00027};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00027};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00027}; Reference proteome {ECO:0000313|Proteomes:UP000198736}.
FT   DOMAIN          7..188
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          250..441
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        332
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00027"
FT   SITE            435
FT                   /note="Increases nucleophilicity of active site Cys"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00027"
SQ   SEQUENCE   466 AA;  50264 MW;  7B289223905A10FE CRC64;
     MKQYPRLVIA GTSSGVGKTT ATLAILAALR EQGRLVQPFK AGPDFIDPSH HRAATGRLSR
     NLDGWMLGPE RNRSIFARAA ADADISMIEG MMGLFDGSSP VNEIGSTAEL AKQLNAPVLL
     VVDGSAMARS AAAMVAGYAR FDPALRVAGV LFNRVGSDGH YQLLKAAVER ETEVIPVGYL
     RPDVALTIPD RHLGLVMAME QGDGRLYHRL AKAALETIDL DRIETLAHST GTLPEALSPP
     VIKSQGRTVR IGVAQDQAFC FYYPDNLESL EAAGAELITF SPLRDVTLPD VEMLYLGGGY
     PEVYGATLAE NRAMRAAVRR FAERGGVIYA ECGGLMYLTE SIRDFDGRPH EMVGIFPAQA
     VMRKPGLTLG YRTVECSRRC ILGEVGVTAR GHEFHYSTLV AKGPLQYACA SRDAEGFLKG
     QDGLMKENVL ALYTHLHFAG RPQVGTALVE AARQSTVRMA RGKGSS
//
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