COBQ_ACIET
ID COBQ_ACIET Reviewed; 496 AA.
AC B9MD32;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Dtpsy_2529;
OS Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Diaphorobacter.
OX NCBI_TaxID=535289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TPSY;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.;
RT "Complete sequence of Diaphorobacter sp. TPSY.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes amidations at positions B, D, E, and G on
CC adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine,
CC and one molecule of ATP is hydrogenolyzed for each amidation.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
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DR EMBL; CP001392; ACM33964.1; -; Genomic_DNA.
DR RefSeq; WP_015913897.1; NC_011992.1.
DR AlphaFoldDB; B9MD32; -.
DR STRING; 535289.Dtpsy_2529; -.
DR EnsemblBacteria; ACM33964; ACM33964; Dtpsy_2529.
DR KEGG; dia:Dtpsy_2529; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_1_4; -.
DR OMA; DVRMNPL; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000450; Chromosome.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01750; GATase1_CobQ; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00028; CobQ; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR InterPro; IPR033949; CobQ_GATase1.
DR InterPro; IPR004459; CobQ_synth.
DR InterPro; IPR011698; GATase_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21343:SF1; PTHR21343:SF1; 1.
DR Pfam; PF01656; CbiA; 1.
DR Pfam; PF07685; GATase_3; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00313; cobQ; 1.
DR PROSITE; PS51274; GATASE_COBBQ; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Glutamine amidotransferase.
FT CHAIN 1..496
FT /note="Cobyric acid synthase"
FT /id="PRO_1000116906"
FT DOMAIN 264..458
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 345
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 450
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 496 AA; 52083 MW; A209E857A5E5572D CRC64;
MSARCIMVLG TTSGAGKSWL ATALCRHYSN QGLKVAPFKA QNMSNNARVV AAPGGEGSEA
GGFGAWGEIG SAQYFQALAA RAVPDVRMNP LLLKPEADTH SQVVLLGQVS DALSQMPWRG
RSEKVWPQIA AALDALRAEN DVVVIEGAGS PAEINLHASD IVNMRVARHA QARCLLVTDI
DRGGAFAHLY GTWALLPADE RALIAGFVLN KFRGDEALLA PAPQMLQDKT GVPVVATIPM
QWDHGLPEED GVFDDRARAS GAVHTRIAVV AYPRISNLDE FQPLKNVPGV RLSWARSPAD
VHGADWIILP GSKATAADLA WLRAQGLDAA IAAHAARGGR VLGVCGGLQM LGEALIDTVG
VDGNGPGLGL LPLVTSFEAT KTVRPTRQCF GAVQGAWRHL AGVAVQGYEI HHGQTAQHPA
MAASGDVARE LIPGLAWQNP GGNVLGLYLH GLFEDAAVLR ALFGADAPTL DAVFEGLAAG
IARHFEPGVL DALAVQ
