COBQ_ALIFM
ID COBQ_ALIFM Reviewed; 495 AA.
AC B5ET63;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028};
GN OrderedLocusNames=VFMJ11_A0326;
OS Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=388396;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ11;
RA Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT "Complete sequence of Vibrio fischeri strain MJ11.";
RL Submitted (AUG-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; CP001133; ACH63591.1; -; Genomic_DNA.
DR RefSeq; WP_012534788.1; NC_011186.1.
DR AlphaFoldDB; B5ET63; -.
DR SMR; B5ET63; -.
DR EnsemblBacteria; ACH63591; ACH63591; VFMJ11_A0326.
DR KEGG; vfm:VFMJ11_A0326; -.
DR HOGENOM; CLU_019250_2_2_6; -.
DR OMA; EIHHGVA; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001857; Chromosome II.
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..495
FT /note="Cobyric acid synthase"
FT /id="PRO_1000090252"
FT DOMAIN 249..442
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 434
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 495 AA; 54302 MW; D1F3676CDCBC2A09 CRC64;
MRKYSPLMVQ GTTSDAGKTV LVAGLCRLLA NKGIQVAPFK PQNMALNSAV TEDGGEIGRA
QALQADAARV KPHVHMNPIL LKPNTDIGAQ VIVQGKAIET MDAWGFHDYK KLAMPYVLES
FSYLSNNYEC VVIEGAGSPA EINLRENDIA NMGFAEAADV PVIIVADIDR GGVFAHLYGT
LALLSESEQA RVKGFVINRF RGDISLLVPG LEWLEEKTGK PVLGVIPYLH GLNLEAEDAI
KSEQLDKGKF VVKVPVVTRI SNHTDFDPLR LHPDIDLQFI GKGESLSGAD FIILPGSKSV
QADLDYVKSQ RWDKDIERHL RYGGKVMGIC GGYQMLGEYL ADPLGIEGAP CSIKGLGYLS
ISTELQKQKQ LTLVEGKLVL PNQSAVKVKG YEIHAGVSTN LGQEHRPISI HTKDAMRYDG
TINSENSIFG TYLHGVFDEP EAFEAILTWA GLEKCQAINM HDIQEEAIER IAKSMEESLD
LSLIWPDVFE KNKAY
