ID COBQ_PSE14 Reviewed; 486 AA.
AC Q48FJ7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=PSPPH_3697;
OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=264730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1448A / Race 6;
RX PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005;
RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M.,
RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J.,
RA Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R.,
RA Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M.,
RA Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A.,
RA Buell R.;
RT "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT 1448A reveals divergence among pathovars in genes involved in virulence and
RT transposition.";
RL J. Bacteriol. 187:6488-6498(2005).
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; CP000058; AAZ37592.1; -; Genomic_DNA.
DR RefSeq; WP_011169237.1; NC_005773.3.
DR AlphaFoldDB; Q48FJ7; -.
DR SMR; Q48FJ7; -.
DR KEGG; psp:PSPPH_3697; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_6; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000551; 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; cd05389; CobQ_N; 1.
DR CDD; cd01750; GATase1_CobQ; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR047045; CobQ_N.
DR InterPro; IPR004459; CobQ_synth.
DR InterPro; IPR011698; GATase_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00313; cobQ; 1.
DR PANTHER; PTHR21343:SF1; COBYRIC ACID SYNTHASE; 1.
DR PANTHER; PTHR21343; DETHIOBIOTIN SYNTHETASE; 1.
DR Pfam; PF01656; CbiA; 1.
DR Pfam; PF07685; GATase_3; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51274; GATASE_COBBQ; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Glutamine amidotransferase.
FT CHAIN 1..486
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332376"
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 486 AA; 52240 MW; 0D402F6C15A5D6F1 CRC64;
MTTLMVQGTT SDAGKSTLVT ALCRWLTRQG VKVVPFKPQN MALNSAVTAD GGEIGRAQAV
QAQACFLQPH TDMNPVLLKP NSDTGAQVII HGRAVTTMNA VAYHGYKEIA MQAVLESHRR
LGESYPVIMV EGAGSPAEIN LRANDIANMG FAEAVDCPVL LIADINRGGV FAHLVGTLEL
LSPSEQARVK GFIINRFRGD IALLQPGLDW LEARTGKPVV GVLPYVMDLH LEAEDGLDQR
QTDKVEHVLN VVVPVLPRIS NHTDFDPLRL HPQVNLQFIG PGQAIPPADL IILPGSKSVR
SDLNYLRNSG WDTAIERHLR YGGKLMGICG GLQMLGEQVH DPLGLEGAAG SSAGFGLLAM
STVLEAEKQL RNVRGRLTLE DAEVSGYEIH AGVTTGPALE QAAVQLDDGR CDGAQSVDGQ
VLGTYLHGLF ESPAACSALL RWAGLANVQS VDYHALRERD IERLADLVEK HLDGPLLREL
CGLEAN
//
