COBQ_BURCM
ID COBQ_BURCM Reviewed; 488 AA.
AC Q0BCS3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Bamb_2494;
OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS (strain AMMD)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=339670;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-244 / AMMD;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA Ramette A., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL Submitted (AUG-2006) 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=ABI88050.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000440; ABI88050.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q0BCS3; -.
DR SMR; Q0BCS3; -.
DR STRING; 339670.Bamb_2494; -.
DR EnsemblBacteria; ABI88050; ABI88050; Bamb_2494.
DR KEGG; bam:Bamb_2494; -.
DR PATRIC; fig|339670.21.peg.2417; -.
DR eggNOG; COG1492; Bacteria.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000662; 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.
FT CHAIN 1..488
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332324"
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; 51704 MW; 0EB3611DE4D5D3FD CRC64;
MIQGTTSDAG KSTLVAGLCR LARRAGARVA PFKPQNMALN SAVTADGGEI GRAQALQALA
AGVAPHTDFN PVLLKPTSDR GAQVIIHGKA RMNLDARAYH DYKPVAFDAV LESYARLRAG
YDTVLVEGAG SPAEINLREG DIANMGFAER VDCPVVLVAD IDRGGVFAHL VGTLACLSDS
ERARVRGFVI NRFRGDIKLL EPGLDWLRAQ TGKPVFGVLP YLHGLLLDAE DMLPSQARSA
AARGDAGVLR VVVPALPRIS NHTDFDPLRA HPQVEFTYWK SGPVPDADLL ILPGSKSVQR
DLAWLRDAGW DAVIRRHLRY GGKVIGICGG MQMLGRTLDD PLGLEGAPAS VPGLGLLDFD
TTLQPDKTLK NVTGHLALPG AAAVHGYEIH MGDTRGPALA APALTLAAGD ASGGVRPDGA
VSADGQILAT YVHGLFDAPD ACAVLLAWAG LDGAERIDYP ALREASLERL ADSFAEHLDL
RALYAEFR