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ID E3J9Z6_FRAIE Unreviewed; 482 AA.
AC E3J9Z6;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 08-MAY-2019, entry version 53.
DE RecName: Full=Hydrogenobyrinate a,c-diamide synthase {ECO:0000256|HAMAP-Rule:MF_00027};
DE EC=6.3.5.9 {ECO:0000256|HAMAP-Rule:MF_00027};
DE AltName: Full=Hydrogenobyrinic acid a,c-diamide synthase {ECO:0000256|HAMAP-Rule:MF_00027};
GN Name=cobB {ECO:0000256|HAMAP-Rule:MF_00027};
GN OrderedLocusNames=FraEuI1c_0475 {ECO:0000313|EMBL:ADP78558.1};
OS Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c).
OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP78558.1, ECO:0000313|Proteomes:UP000002484};
RN [1] {ECO:0000313|EMBL:ADP78558.1, ECO:0000313|Proteomes:UP000002484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45817 / CECT 9037 / EuI1c
RC {ECO:0000313|Proteomes:UP000002484};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA Beauchemin N., Sen A., Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT "Complete sequence of Frankia sp. EuI1c.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ATP-dependent amidation of the two
CC carboxylate groups at positions a and c of hydrogenobyrinate,
CC using either L-glutamine or ammonia as the nitrogen source.
CC {ECO:0000256|HAMAP-Rule:MF_00027}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + 2 H2O + hydrogenobyrinate + 2 L-glutamine = 2 ADP
CC + 2 H(+) + hydrogenobyrinate a,c-diamide + 2 L-glutamate + 2
CC phosphate; Xref=Rhea:RHEA:12544, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:77873,
CC ChEBI:CHEBI:77874, ChEBI:CHEBI:456216; EC=6.3.5.9;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00027};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00027};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step
CC 9/10. {ECO:0000256|HAMAP-Rule:MF_00027}.
CC -!- DOMAIN: Comprises of two domains. The C-terminal domain contains
CC the binding site for glutamine and catalyzes the hydrolysis of
CC this substrate to glutamate and ammonia. The N-terminal domain is
CC anticipated to bind ATP and hydrogenobyrinate and catalyzes the
CC ultimate synthesis of the diamide product. The ammonia produced
CC via the glutaminase domain is probably translocated to the
CC adjacent domain via a molecular tunnel, where it reacts with an
CC activated intermediate. {ECO:0000256|HAMAP-Rule:MF_00027}.
CC -!- MISCELLANEOUS: The a and c carboxylates of hydrogenobyrinate are
CC activated for nucleophilic attack via formation of a
CC phosphorylated intermediate by ATP. CobB catalyzes first the
CC amidation of the c-carboxylate, and then that of the a-
CC 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; CP002299; ADP78558.1; -; Genomic_DNA.
DR RefSeq; WP_013421680.1; NC_014666.1.
DR STRING; 298654.FraEuI1c_0475; -.
DR EnsemblBacteria; ADP78558; ADP78558; FraEuI1c_0475.
DR KEGG; fri:FraEuI1c_0475; -.
DR eggNOG; ENOG4105C0Y; Bacteria.
DR eggNOG; COG1797; LUCA.
DR HOGENOM; HOG000289958; -.
DR KO; K02224; -.
DR OMA; QPFKCGP; -.
DR OrthoDB; 692368at2; -.
DR BioCyc; FSP298654:G1GOT-473-MONOMER; -.
DR UniPathway; UPA00148; UER00220.
DR Proteomes; UP000002484; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042242; F:cobyrinic acid a,c-diamide synthase activity; IEA:InterPro.
DR GO; GO:0043802; F:hydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing) 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 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; IPR017929; CobB/CobQ_GATase.
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;
DR PRODOM; E3J9Z6.
DR SWISS-2DPAGE; E3J9Z6.
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00027};
KW Cobalamin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00027,
KW ECO:0000256|PROSITE-ProRule:PRU00606};
KW Complete proteome {ECO:0000313|Proteomes:UP000002484};
KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00027,
KW ECO:0000256|PROSITE-ProRule:PRU00606, ECO:0000256|SAAS:SAAS00056751};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00027};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00027};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00027};
KW Reference proteome {ECO:0000313|Proteomes:UP000002484}.
FT DOMAIN 262 460 GATase cobBQ-type. {ECO:0000259|PROSITE:
FT PS51274}.
FT ACT_SITE 345 345 Nucleophile. {ECO:0000256|HAMAP-Rule:
FT MF_00027}.
FT SITE 452 452 Increases nucleophilicity of active site
FT Cys. {ECO:0000256|HAMAP-Rule:MF_00027}.
SQ SEQUENCE 482 AA; 48617 MW; B849D967E5F26F21 CRC64;
MRIPRVVLAA PASGAGKTSI ATGLLAALRA RGLAVSPHKV GPDYIDPSYH ALAAGRPGRN
LDPWLVGEQR VAPLFLHGAL HPRRADVAVV EGVMGLFDGH ATRAGFGSTA HVATLLAAPV
VLVVDARSAG RSVAATVHGF RSFDPAVRIG GVVLNQVGTE RHAEILRAAM AEIGMPVLGV
LGRRPDLVTP SRHLGLVPAA ERAAPARDAV AELGAAVGSG LDLDALLALA ATAPDLPAEP
WDARVAALEP VGSPVPAGPR PVVAVAGGPA FTFGYAETPE LLAAAGAEVV GFDPTVDEAL
PAGTSGLIIG GGFPEVHAGA LAANAALRSR VRAFAATGAP VAAECAGLLY LSSALDGAPM
CGVLGEVTAA MTPRLTLGYR EAAAVTDSVL AARGTTVHGH EFHRTVATPA AGGSTGGDAR
RGAAPAWRWR DASGVEVAEG FVRGAIHASY LHTHWAGVPG AAHRFVAAAR AAHQTEAFRA
AG
//
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