COBQ_BURVG
ID COBQ_BURVG Reviewed; 488 AA.
AC A4JGX5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028};
GN OrderedLocusNames=Bcep1808_2530;
OS Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS (strain R1808)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=269482;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G4 / LMG 22486;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4.";
RL Submitted (MAR-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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABO55528.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000614; ABO55528.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A4JGX5; -.
DR SMR; A4JGX5; -.
DR STRING; 269482.Bcep1808_2530; -.
DR EnsemblBacteria; ABO55528; ABO55528; Bcep1808_2530.
DR KEGG; bvi:Bcep1808_2530; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_4; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002287; Chromosome 1.
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; Reference proteome.
FT CHAIN 1..488
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332325"
FT DOMAIN 248..441
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 328
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 433
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 488 AA; 51756 MW; C5DCDF841070D09D CRC64;
MIQGTTSDAG KSTLVAGLCR LARRAGARVA PFKPQNMALN SAVTADGGEI GRAQALQALA
AGVAPHTDFN PVLLKPTSDR GAQVIIHGAA RMNLDARAYH DYKPVAFDAV LESYARLRAG
YDTVIVEGAG SPAEINLRDG DIANMGFAER VDCPVVLVAD IDRGGVFAHL VGTLACLSDS
ERARVRGFVI NRFRGDIGLL EPGLDWLRAQ TGKPVFGVLP YLHGLLLDAE DMLPRQARSA
ATRDGAGVLR VVVPALPRIS NHTDFDPLRA HPQVEFTYWK SGPVPAADLL ILPGSKSVQR
DLQWLRDAGW DTVIRRHLRY GGKVIGICGG MQMLGRTLDD PLGLEGAPGS VPGLGLFDFD
TTLLPHKTLK NVTGQLALPG APAVRGYEIH MGDTRGPALA APALQLAADD AAGGSRADGA
LSADGQLLAT YVHGLFDTPA ACAALLAWAG LDGGERIDYP ALREASIERL ADSFAEHLDL
RALYAEFR