COBQ_PSEPW
ID COBQ_PSEPW Reviewed; 484 AA.
AC B1J1N6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028};
GN OrderedLocusNames=PputW619_1236;
OS Pseudomonas putida (strain W619).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=390235;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W619;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA Richardson P.;
RT "Complete sequence of Pseudomonas putida W619.";
RL Submitted (FEB-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; CP000949; ACA71741.1; -; Genomic_DNA.
DR RefSeq; WP_012313151.1; NC_010501.1.
DR AlphaFoldDB; B1J1N6; -.
DR SMR; B1J1N6; -.
DR STRING; 390235.PputW619_1236; -.
DR EnsemblBacteria; ACA71741; ACA71741; PputW619_1236.
DR KEGG; ppw:PputW619_1236; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_0_6; -.
DR OMA; GREVHDP; -.
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..484
FT /note="Cobyric acid synthase"
FT /id="PRO_1000090240"
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; 51631 MW; 2C7222F732635270 CRC64;
MTTLMVQGTT SDAGKSTLVT ALCRWLLRQG VAVVPFKPQN MALNSAVTAD GGEIGRAQAV
QAQACRLAPH TDMNPVLLKP NSDTGAQVII HGRAVTSMNA VAYHDYKAIA MQAVLASHQR
LSGEYPVVMV EGAGSPAEIN LRAGDIANMG FAEAVDCPVI LVADINRGGV FAHLVGTLEL
LSPTEQARVK GFVINRFRGD IALLQPGLDW LEQRTGKPVL GVLPYVTDLH LEAEDGIDVR
QGAKDERVLK VIVPVLPRIS NHTDFDPLRL HPQVDLQFIG PGQPIPPADL IILPGSKSVR
GDLAQLRERG WDTAIARHLR YGGKLIGICG GLQMLGREVH DPLGLEGPAG SSPGLGLLDY
ATVLEAQKQL RNVAGALSLE QSPVAGYEIH AGVTQGPALQ RPAVQLADGR SDGAISADGQ
ILATYLHGLF EGSQSCAALL RWAGLADVQQ IDYEALRERD IERLADLVEK HLDTAHLRKL
CGVA
