COBQ_PSEU5
ID COBQ_PSEU5 Reviewed; 485 AA.
AC A4VJ40;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=PST_1297;
OS Pseudomonas stutzeri (strain A1501).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=379731;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1501;
RX PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT "Nitrogen fixation island and rhizosphere competence traits in the genome
RT of root-associated Pseudomonas stutzeri A1501.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
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; CP000304; ABP78991.1; -; Genomic_DNA.
DR RefSeq; WP_011912475.1; NC_009434.1.
DR AlphaFoldDB; A4VJ40; -.
DR SMR; A4VJ40; -.
DR STRING; 379731.PST_1297; -.
DR EnsemblBacteria; ABP78991; ABP78991; PST_1297.
DR KEGG; psa:PST_1297; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_6; -.
DR OMA; GREVHDP; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000233; 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; Reference proteome.
FT CHAIN 1..485
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332375"
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 485 AA; 51519 MW; CC1CA4670ED14059 CRC64;
MTTLMVQGTT SDAGKSTLVT ALCRWLARQG VAVVPFKPQN MALNSAVTAD GGEIGRAQAV
QAQAANLAPH TDMNPVLLKP NSDIGAQVIV HGRAVTSMDA AAYHDYKRVA LQAVLDSHRR
LSAAYRVVMV EGAGSPAEIN LRAGDIANMG FAEAVDCPVI LIADIDKGGV FAHLVGTLAL
LSESEQARVQ GFVINRFRGD IALLQPGLDW LEQRTGKPVL GVLPYLMDLH LEAEDAIDVR
QAGKSAEVLK VVVPVLPRIS NHTDFDPLRL HPQVDLQFVG PGQPVPSADL IILPGSKSVR
ADLAWLRANG WEAAIQKHLR YGGKLLGICG GLQMLGTRIA DPLGLEGPAG ESAGLGLLDF
ATVLEADKQL RNVQGRLLPE AVPVTGYEIH AGVSTGSALA RPAVQLDDGR SDGAISADGQ
ILGTYLHGLF ESPDACAALL RWAGLEAVQQ VDYHALRERD IERLADLVET HLDTAKLRRF
CGLGG