ID A0A2S5JLV7_9RHOB Unreviewed; 480 AA.
AC A0A2S5JLV7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|ARBA:ARBA00019833, ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=LV82_00402 {ECO:0000313|EMBL:PPB82469.1};
OS Albidovulum inexpectatum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Albidovulum.
OX NCBI_TaxID=196587 {ECO:0000313|EMBL:PPB82469.1, ECO:0000313|Proteomes:UP000239736};
RN [1] {ECO:0000313|EMBL:PPB82469.1, ECO:0000313|Proteomes:UP000239736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12048 {ECO:0000313|EMBL:PPB82469.1,
RC ECO:0000313|Proteomes:UP000239736};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (JAN-2018) 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:0000256|ARBA:ARBA00025166, ECO:0000256|HAMAP-Rule:MF_00028}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004953, ECO:0000256|HAMAP-Rule:MF_00028}.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC {ECO:0000256|ARBA:ARBA00006205, ECO:0000256|HAMAP-Rule:MF_00028}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PPB82469.1}.
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DR EMBL; PRDS01000001; PPB82469.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5JLV7; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000239736; Unassembled WGS sequence.
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-UniRule.
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 {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW Rule:MF_00028};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|HAMAP-Rule:MF_00028};
KW Reference proteome {ECO:0000313|Proteomes:UP000239736}.
FT DOMAIN 4..236
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 250..433
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 427
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 480 AA; 51186 MW; DF19572F1A5E5105 CRC64;
MTAVMIQGCG SNVGKSLLVA GLCRAARRRG LSVAPFKPQN MSNNAAVTLD GGEIGRAQAL
QALACGLQPH TDMNPVLLKP ETDTGAQVVV QGRRVATVRA RDYARLKPQL LQPVLDSFQR
LRDAHDLVIV EGAGSPAEVN LRADDIANMG FARAANVPVI LVGDIDRGGV IAQIVGTQAV
LDDGDAAMVR GFIINKFRGD PRLFDDGYRL IEDRTGWRGL GVVPFFPEAS RLPAEDALDL
TRGGGGGPVR IACLALSRIA NFDDLDPLRI EPCVDLVMVR QGEAIPGDRD LVIIPGSKST
RGDLDFLRAQ GWDIDLRAHI RRGGQVLGIC GGYQMLGRTI ADPEGIEGPA GESPGLGLLD
VRTVMTADKR LTRTDAVHAP TGQKMQGYEI HIGRTEGPDC ARPFALVDGR PEGAISPDGR
VMGSYLHGIF GSDGFRAAFL SRFGGSAGID YGFEVRRVLD LLADHVEANL DVDRLLGIAN
//
