COBQ_METPB
ID COBQ_METPB Reviewed; 488 AA.
AC B1Z9X0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Mpop_5262;
OS Methylorubrum populi (strain ATCC BAA-705 / NCIMB 13946 / BJ001)
OS (Methylobacterium populi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=441620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-705 / NCIMB 13946 / BJ001;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marx C., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium populi BJ001.";
RL Submitted (APR-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; CP001029; ACB83356.1; -; Genomic_DNA.
DR RefSeq; WP_012456952.1; NC_010725.1.
DR AlphaFoldDB; B1Z9X0; -.
DR SMR; B1Z9X0; -.
DR STRING; 441620.Mpop_5262; -.
DR EnsemblBacteria; ACB83356; ACB83356; Mpop_5262.
DR KEGG; mpo:Mpop_5262; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_0_5; -.
DR OMA; EIHHGVA; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000007136; 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; 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; 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..488
FT /note="Cobyric acid synthase"
FT /id="PRO_1000090234"
FT DOMAIN 252..440
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 334
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 432
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 488 AA; 51827 MW; B8887039910B2517 CRC64;
MTRALMIQGT GSDVGKSLLV AGLARAFTRR GLRVRPFKPQ NMSNNAAVTA DGGEIGRAQA
LQARAARVAP SVHMNPVLLK PQSEVGAQVV VQGRMIGTAR ARDYQAWKPR LMESVLDSFE
RLRADSDLVL VEGAGSPAEV NLRRGDIANM GFARATDTPV VIVGDIDRGG VIASLVGTQA
VMEPDDAAMI RGFIVNRFRG DPTLFADGMA LIAERTGWTP FGLVPFFPEA GRLPPEDAVA
LDVAGAGRDG SVPLIAVLRF PHIANFDDLD PLRQEPGVSV AFVPAGEPIP AEADLIVLPG
SKTTIDDLDF LRAQGWDIDI RAHLRRGRRV LGLCGGYQML GRAIADPQGI EGAPRALPGL
GLLDVETVMT AEKRLVAVTG TTLADDEPFS GYEMHVGDTT GPDAAHPLLR FADGRADGAV
SADGLVAGTY VHGLFANDRQ RAAWLARLGA APGLTNYEAG IEAVLDRFAD HLEAHLDCDG
LLRLCRPL