COBQ_PSEMY
ID COBQ_PSEMY Reviewed; 483 AA.
AC A4XT53;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Pmen_1755;
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ymp;
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., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) 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; CP000680; ABP84519.1; -; Genomic_DNA.
DR RefSeq; WP_012018259.1; NC_009439.1.
DR AlphaFoldDB; A4XT53; -.
DR SMR; A4XT53; -.
DR STRING; 399739.Pmen_1755; -.
DR EnsemblBacteria; ABP84519; ABP84519; Pmen_1755.
DR KEGG; pmy:Pmen_1755; -.
DR PATRIC; fig|399739.8.peg.1779; -.
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..483
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332372"
FT DOMAIN 248..434
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 426
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 483 AA; 51911 MW; 3B8685C485A9E052 CRC64;
MPTLMVQGTT SDAGKSTLVT ALCRWARRQG VSVAPFKPQN MALNSAVTAD GGEIGRAQAV
QAQAAGLAPH TDMNPVLLKP NSDMGAQVII HGRAIGNMQA LTYHGYKPVA MAAVLESHAR
LVERHQLVLV EGAGSPAEIN LRAGDIANMG FAEAVDCPVI LIADIDKGGV FAHLVGTLEL
LSPSEQARIR GFVINRFRGD IALLKPGLDW LEQRTGKPVL GVLPYLTDFH LEAEDAVDTR
QQAKSAQALR VVVPVLPRIS NHTDFDPLRL HPQVQLTFVG PGQAIPPADL IILPGSKSVR
ADLARLREQG WDTAIARHLR YGGKLLGICG GLQMLGRQIH DPHGLEGAAG SSEGLGLLDF
ETVLEPEKQL RNVRGQLCLE QAQVSGYEIH AGVSRGPGLN GAVQLDDGRS DGGLSADGQV
LGTYLHGLFE QPSAFAALLR WAGLHEVQTV DYQALRERDI ERLADQVELH LDNEQLRMLC
GIR
