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Database: UniProt
Entry: A0A0M4SQ25_9NOSO
LinkDB: A0A0M4SQ25_9NOSO
Original site: A0A0M4SQ25_9NOSO 
ID   A0A0M4SQ25_9NOSO        Unreviewed;       480 AA.
AC   A0A0M4SQ25;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=cbiA {ECO:0000256|HAMAP-Rule:MF_00027};
GN   ORFNames=ACX27_26570 {ECO:0000313|EMBL:ALF55598.1};
OS   Nostoc piscinale CENA21.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=224013 {ECO:0000313|EMBL:ALF55598.1, ECO:0000313|Proteomes:UP000062645};
RN   [1] {ECO:0000313|Proteomes:UP000062645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CENA21 {ECO:0000313|Proteomes:UP000062645};
RA   Leao T.F., Leao P.N., Guimaraes P.I., de Melo A.G.C., Ramos R.T.J.,
RA   Silva A., Fiore M.F., Schneider M.P.C.;
RT   "Genome Of Nitrogen-Fixing Cyanobacterium Nostoc piscinale CENA21 From
RT   Solimoes/Amazon River Floodplain Sediments And Comparative Genomics To
RT   Uncover Biosynthetic Natural Products Potential.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALF55598.1, ECO:0000313|Proteomes:UP000062645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CENA21 {ECO:0000313|EMBL:ALF55598.1,
RC   ECO:0000313|Proteomes:UP000062645};
RX   PubMed=27034496;
RA   Leao T., Guimaraes P.I., de Melo A.G., Ramos R.T., Leao P.N., Silva A.,
RA   Fiore M.F., Schneider M.P.;
RT   "Draft Genome Sequence of the N2-Fixing Cyanobacterium Nostoc piscinale
RT   CENA21, Isolated from the Brazilian Amazon Floodplain.";
RL   Genome Announc. 4:0-0(2016).
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; CP012036; ALF55598.1; -; Genomic_DNA.
DR   RefSeq; WP_062296901.1; NZ_CP012036.1.
DR   AlphaFoldDB; A0A0M4SQ25; -.
DR   STRING; 224013.ACX27_26570; -.
DR   PATRIC; fig|224013.5.peg.6363; -.
DR   OrthoDB; 9764035at2; -.
DR   UniPathway; UPA00148; UER00231.
DR   Proteomes; UP000062645; 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-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; 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   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}.
FT   DOMAIN          3..195
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          258..450
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        341
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00027"
FT   SITE            444
FT                   /note="Increases nucleophilicity of active site Cys"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00027"
SQ   SEQUENCE   480 AA;  53108 MW;  7364EE6B0432C8FC CRC64;
     MALVIAGERS GVGKTTVTLT LLASLCRRGG QVQSFKVGPD YIDPMFHRYV TGLACRNLDP
     VLTSEAYVQQ CFAHHSQASE YALVEGVMGL FDGIGSREEN TLHPFTFAST AHIAKLLDLP
     VVLVIDCSRL SGSVAAIAHG YCTFDPKIKI AGLVLNRVGS DRHLSLLKDA LKSLQLPILG
     VLRRQDNITI PDRHLGLVPT AELSELDAVI ERLADLGDTC FDWQSLLPLL RQKGDKGDKE
     DKGENNPGCL GKSSSVVRVA VACDRAFNFY YQDNLDLLQK LGAELVFWSP LEDAELPRNI
     QGMYFGGGFP EVFAQQLTKN INVLQAVKTA IIQGIPTIAE CGGLMYLCRE IIDFEGKSYP
     MVGIIPTSAC MDKRLTLGYR RAVALQDSLL VNAGTNVYGH EFHRSTLKAN SRQPLFDTYR
     YDCDENMGFE GWNLPINLHA SYIHLHWGSN GEIPQRFLQQ CQSYSVSHSS EVLTRIINRR
//
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