COBQ_PSEAB
ID COBQ_PSEAB Reviewed; 490 AA.
AC Q02JB8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=PA14_47690;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ10465.1; -; Genomic_DNA.
DR RefSeq; WP_003112202.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02JB8; -.
DR SMR; Q02JB8; -.
DR PRIDE; Q02JB8; -.
DR EnsemblBacteria; ABJ10465; ABJ10465; PA14_47690.
DR KEGG; pau:PA14_47690; -.
DR HOGENOM; CLU_019250_2_2_6; -.
DR OMA; EIHHGVA; -.
DR BioCyc; PAER208963:G1G74-4007-MON; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000653; 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..490
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332368"
FT DOMAIN 252..439
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 333
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 431
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 490 AA; 52349 MW; 8C1D9B618A2B2750 CRC64;
MSDRGRTLMV QGTTSDAGKS TLVTALCRWL ARRGVAVVPF KPQNMALNSA VTADGGEIGR
AQAVQAQACR LAPHTDMNPV LLKPNTDIGA QVIIHGRAVT SMDAAAYHDY KRVAMEAVLA
SHGRLAAAYR VVMVEGAGSP AEINLRANDI ANMGFAEAVD CPVILVADID RGGVFAHLVG
TLELLSDSER ERVKGFVINR FRGDIALLQP GLDWLEARTG KPVLGVLPYV SDLHLEAEDA
IDTRQAAKVG PRLKVVVPVL PRISNHTDFD PLRLHPQVEL SFVGPGQALP SADLIVLPGS
KSVRADLAAL RERGWDEAIL RHLRYGGRLL GICGGLQMLG ERLHDPLGLE GAAGSSAGLG
LLALETTLEA DKQLRNVQGR LSLEDAPLSG YEIHAGVTRG EALARPAVVL DDGRADGARS
VDGNVMGTYL HGLFESTAAC SALLRWAGLR EVQAVDYQAL RERDIERLAD LVERNLDTGR
LLALCGEPHA
