ID A0A2W2DCF0_9ACTN Unreviewed; 515 AA.
AC A0A2W2DCF0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=C1I99_13185 {ECO:0000313|EMBL:PZF98509.1};
OS Micromonospora deserti.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=2070366 {ECO:0000313|EMBL:PZF98509.1, ECO:0000313|Proteomes:UP000248749};
RN [1] {ECO:0000313|EMBL:PZF98509.1, ECO:0000313|Proteomes:UP000248749}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13K206 {ECO:0000313|EMBL:PZF98509.1,
RC ECO:0000313|Proteomes:UP000248749};
RA Sahin N., Saygin H., Ay H.;
RT "Draft genome sequence of Salinispora sp. 13K206.";
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|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|HAMAP-Rule:MF_00028}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
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:PZF98509.1}.
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DR EMBL; POUB01000074; PZF98509.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W2DCF0; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000248749; 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.
DR PROSITE; PS51273; GATASE_TYPE_1; 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:UP000248749}.
FT DOMAIN 6..234
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 261..441
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 340
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 434
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 515 AA; 53611 MW; 92F9A0DB1C193704 CRC64;
MSGGLLVAGT TSDAGKSVLT AGICRWLHRQ GVKVAPFKAQ NMSNNSAVVV GPDGRGGEIG
RAQAMQAAAC GLAPDLRFNP VLLKPGSDLA SQVVLLGEAV DTVTAGNFRE LRPRLAQTAF
AALAALRAEY DVVICEGAGS PAEINLRAGD YVNMGLARHA GLPTIVVGDI DRGGVFASMF
GTVALLDPAD QALIAGFVVN KFRGDLGLLR PGLEMLHRVT GRPTYGVLPW ALDLWLDAED
SLAYGRVLGR PAAPHGTEWL DVAVVRLPRI SNATDVEALA TEPGVRVRLT VEPAELAAAD
LVVLPGSKST VADLAWLRRS GLADAVLAHA AAGRPLLGIC GGFQMLARAI HDPVESRQGS
VPGLGLLPIE ITFDPRKTVR QSTGTVGGNV AVRGYEIHHG YVSSADPALV PLLTCADGTG
EGVVLGAVHG THWHGAFESD AFRRRFLTEV ARLAGRTGFR VAPGTAFAAA RERSLDLLGD
LVEEHLDTDA LRRLIEAGAP AGLPFIPPGA PPAAG
//