ID COBQ_NOVAD Reviewed; 491 AA.
AC Q2GBK2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Saro_0323;
OS Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS 56034 / CIP 105152 / NBRC 16084 / F199).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=279238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084 /
RC F199;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
RA Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
RL Submitted (JAN-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}.
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DR EMBL; CP000248; ABD24771.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2GBK2; -.
DR SMR; Q2GBK2; -.
DR STRING; 279238.Saro_0323; -.
DR KEGG; nar:Saro_0323; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_5; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000009134; 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; Reference proteome.
FT CHAIN 1..491
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332357"
FT DOMAIN 246..432
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 424
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 491 AA; 51104 MW; 580C3DCA3F8D5ECD CRC64;
MLQGTGSDVG KSVLVAGLCR ALVQRGLRVL PFKPQNMSNN AAVTSDGGEI GRAQALQAIA
CKVEPHTDMN PVLLKPQADR TSQLIVHGRV RGTLGAGNFR QARGALLGEV LASYNRLRRA
CDIVVVEGAG SPAEINLRAG DIANMGFARA AGVPVVLVGD IDRGGVIAAI VGTRTIIDPA
DTAMIQGFII NKFRGDPALF ADGYAQIESL SGWRGFGVVP WLSAAARLPS EDAVVLESGK
ARAESRKLIA CPILPRISNF DDLDPLKLEH GVDLHMVPPG QPIPAEAALI ILPGSKSTIA
DLAALRAEGW DIDIFAHHRR GGLILGLCGG YQMLGKSIAD PDGFEGSASA ASGLGLLDVE
TTLHAHKALR PVSGLAMGAP FQGYEMHMGQ TNGPDTEQPF AVFADGRRDG AINAGGTVFG
SYVHGLLADA ELRRALLSRM DVEAGGVDYG ASVEAALDEI AAALEEHLDI DALVALAMAE
RPASVPAGDS A
//
