COBQ_CHLAD
ID COBQ_CHLAD Reviewed; 491 AA.
AC B8G7Y8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Cagg_1259;
OS Chloroflexus aggregans (strain MD-66 / DSM 9485).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=326427;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-66 / DSM 9485;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Foster B., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Bryant D.A., Richardson P.;
RT "Complete sequence of Chloroflexus aggregans DSM 9485.";
RL Submitted (DEC-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001337; ACL24167.1; -; Genomic_DNA.
DR RefSeq; WP_012616531.1; NC_011831.1.
DR AlphaFoldDB; B8G7Y8; -.
DR STRING; 326427.Cagg_1259; -.
DR EnsemblBacteria; ACL24167; ACL24167; Cagg_1259.
DR KEGG; cag:Cagg_1259; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_0; -.
DR OMA; DVRMNPL; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002508; 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..491
FT /note="Cobyric acid synthase"
FT /id="PRO_1000116899"
FT DOMAIN 251..444
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 329
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 436
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 491 AA; 52845 MW; C4CF62587FCA7D0B CRC64;
MPAPVVMVIG TASSVGKSTL VAALCRLAAR RGLRVAPFKA QNMSNNAAVT ADGGEIARST
AVQAAAAGIA PTVAMNPILI KPEGQRRSQI IVEGRPWQTL AAGDFWRRKT LLWEVVTRNL
DALRATYDLV IAEGAGSPVE LNLKAGDIVN MRVAVYAQAR TLLVGDIDRG GIFAQLLGTL
MLLDPTERQL IQGLIVNRFR GDPALFVDGV RILEERSGIP VLGVVPWIED LGLAEEDAVA
IEQSTPVMAQ GITIAVIRLP TIANFDDFDP LAREPGVTVR YIDRPGELAG VAAVIIPGVK
HTIAARRWLR ERGFDEALRR FPGAIVGICG GYQLLGERIS DPLAVEGNGG DEVGLGLLPV
ETIFVTTKQT TQTVAHARVP WGGQAPLHGY EIHMGRTHRI GAASALLTII QRGAQAVLEE
DGCISPDGRV WGCYLHGLFT NDEFRHGWLR QLGWQPTTSV SGSVDPINRL ADHVARALGE
TVLDRLFRLT E