COBQ_PSEPG
ID COBQ_PSEPG Reviewed; 484 AA.
AC B0KT65;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028};
GN OrderedLocusNames=PputGB1_1276;
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1;
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., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
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; CP000926; ABY97183.1; -; Genomic_DNA.
DR RefSeq; WP_012270958.1; NC_010322.1.
DR AlphaFoldDB; B0KT65; -.
DR SMR; B0KT65; -.
DR STRING; 76869.PputGB1_1276; -.
DR EnsemblBacteria; ABY97183; ABY97183; PputGB1_1276.
DR KEGG; ppg:PputGB1_1276; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_6; -.
DR OMA; GREVHDP; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002157; 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..484
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332374"
FT DOMAIN 248..435
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 427
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 484 AA; 51448 MW; B60C72CC614618B7 CRC64;
MTTLMVQGTT SDAGKSTLVT ALCRWLLRQG VGVVPFKPQN MALNSAVTAD GGEIGRAQAV
QAQACRLAPH TDMNPVLLKP NSDTGAQVII HGRAVTSMNA VAYHDYKATA MQAVLASHQR
LSAAYPVVMV EGAGSPAEIN LRAGDIANMG FAEAVDCPVI LVADINRGGV FAHLVGTLEL
LSPSEQARVK GFVINRFRGD IALLQPGLDW LEQRTGKPVL GVLPYVTDLH LEAEDGIDVR
QGAKLARVLK VIVPVLPRIS NHTDFDPLRL HPQVDLQFIG PGQPIPAADL IILPGSKSVR
GDLAQLRERG WDKAIERHLR YGGKLIGICG GLQMLGRQVH DPLGLEGAAG SSQGLGLLDY
ATVLEAEKQL RNVAGTLNLE AAAVAGYEIH AGVTSGPALE RPAVQLADGR CDGAVSADGQ
ILATYLHGLF EGSQSCAALL RWAGLEDVQA IDYEALRERD IERLADLVEK HLDTALLRQL
CGVA
