COBQ_CAUSK
ID COBQ_CAUSK Reviewed; 486 AA.
AC B0SXF9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Caul_2617;
OS Caulobacter sp. (strain K31).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter; unclassified Caulobacter.
OX NCBI_TaxID=366602;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K31;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Stephens C., Richardson P.;
RT "Complete sequence of chromosome of Caulobacter sp. K31.";
RL Submitted (JAN-2008) 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; CP000927; ABZ71744.1; -; Genomic_DNA.
DR RefSeq; WP_012286647.1; NC_010338.1.
DR AlphaFoldDB; B0SXF9; -.
DR SMR; B0SXF9; -.
DR STRING; 366602.Caul_2617; -.
DR EnsemblBacteria; ABZ71744; ABZ71744; Caul_2617.
DR KEGG; cak:Caul_2617; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_5; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
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..486
FT /note="Cobyric acid synthase"
FT /id="PRO_1000074397"
FT DOMAIN 251..439
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 333
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 431
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 486 AA; 50447 MW; E286DFE2AF00AC55 CRC64;
MASLMIQGCG SDVGKSTLVA GLCRLFVNRG LIVRPFKPQN MSNNAAVTED GGEIGRAQAL
QAIACRTPPT VHMNPVLLKP QSDVGAQVVV RGKVVGAYQA RAFQGLKPDL LATTVESYRL
LAAEADLVLV EGAGSPAETN LRAGDIANMG FAHAADVPVA LIGDIDRGHV IAALAGAHLV
LDAADRERIK GFIINKFRGD PSLFDEGRRE IVARTGWPDL GMAPWLASAR ALPAEDAVAL
ERPVREDGGR RAKIVVPMLS RIANFDEFDP LRADPSLDFS FLPPGTPVPG DADLVILPGT
KATLADLTFL RAQGWDIDIL AHARRGGRVL GVCGGYQMLG RTVSDPEGVE GAPGSAPGLG
LLDVETVLLG DKVLRATAGR LVGTDAAFSG YEMHIGRTTG QGAARPMLAF DGGAADGAVS
ADGRVAGAYV HGLFERGEAR AALLAPLGVA ASSGDHAAQV DAALDEIAAV LERSLDIEAI
ARIAGV
