ID Q9F2A0_ALLVI Unreviewed; 458 AA.
AC Q9F2A0;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 102.
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=dsrN {ECO:0000313|EMBL:AAG13086.1};
GN Synonyms=cbiA {ECO:0000256|HAMAP-Rule:MF_00027};
OS Allochromatium vinosum (Chromatium vinosum).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=1049 {ECO:0000313|EMBL:AAG13086.1};
RN [1] {ECO:0000313|EMBL:AAG13086.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=D DSM 180 {ECO:0000313|EMBL:AAG13086.1};
RX PubMed=15687204; DOI=10.1128/JB.187.4.1392-1404.2005;
RA Dahl C., Engels S., Pott-Sperling A.S., Schulte A., Sander J., Lubbe Y.,
RA Deuster O., Brune D.C.;
RT "Novel genes of the dsr gene cluster and evidence for close interaction of
RT Dsr proteins during sulfur oxidation in the phototrophic sulfur bacterium
RT Allochromatium vinosum.";
RL J. Bacteriol. 187:1392-1404(2005).
RN [2] {ECO:0000313|EMBL:AAG13086.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=D DSM 180 {ECO:0000313|EMBL:AAG13086.1};
RA Dahl C.;
RL Submitted (JAN-2006) 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}.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC {ECO:0000256|ARBA:ARBA00006205}.
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DR EMBL; U84760; AAG13086.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9F2A0; -.
DR OMA; CDGVYLP; -.
DR BioCyc; MetaCyc:MONOMER-12382; -.
DR UniPathway; UPA00148; UER00231.
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/CobB_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:SF2; COBYRIC ACID SYNTHASE; 1.
DR PANTHER; PTHR43873; 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 7..187
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 248..439
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00027"
FT SITE 437
FT /note="Increases nucleophilicity of active site Cys"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00027"
SQ SEQUENCE 458 AA; 50473 MW; 4EAA6B7E8750F694 CRC64;
MASLYIAAPQ KSSGKTTLSI GLCREFTRRG LVVQPFKKGP DYIDPLWLGQ AAGRSCFNLD
FHTMSESEIR SAFARELGAA DLGLIEGNVG LFDSTRLDGA HSNAELAKLI GAPVVLVVNC
HGLARGIAPL LQGYLAFDPE LDIAGVILNK VGGGRHGENL VRVVEHYTDL PVLGLLRRTD
EISIDERHLG LMPSNETEDA EVWIERIRAR IADQVDLDRL LEIAEHAPTP EPEPVGVIQP
ARDGDLVRIG IARDAAFGFY YPDDLRALAA GGAELVPFSP ISDSVLPEVD ALFIGGGFPE
YRMAELEDNR LMRQAIRDFV ADDRPLYAEC GGLMYLCSRL CWKGERRSMV GALDADVEMC
DRPQGRGYVR LSETEAFPWP RLESAPPDEI AAHEFHHSAI LKPDPDWRYG YTVRRGTGID
GSHDGIVQGN LLACYSHLRA VGGNRWTDRF LAHIRRTL
//
