ID A0A1C6TJ80_9ACTN Unreviewed; 513 AA.
AC A0A1C6TJ80;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=GA0074692_6456 {ECO:0000313|EMBL:SCL41707.1};
OS Micromonospora pallida.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=145854 {ECO:0000313|EMBL:SCL41707.1, ECO:0000313|Proteomes:UP000198959};
RN [1] {ECO:0000313|EMBL:SCL41707.1, ECO:0000313|Proteomes:UP000198959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43817 {ECO:0000313|EMBL:SCL41707.1,
RC ECO:0000313|Proteomes:UP000198959};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FMHW01000002; SCL41707.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6TJ80; -.
DR STRING; 145854.GA0074692_6456; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000198959; 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}.
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 513 AA; 54113 MW; FD563237775D6071 CRC64;
MSGGLLVAGT TSDAGKSVLT AGICRWLHRR GVKVAPFKAQ NMSNNSAVVV GPDGRGGELG
RAQAMQAAAC GLTPDLRFNP VLLKPGSDLA SQVVLLGEAV DTVTAGNFRV LRPRLAETAY
AALAELRAEY DVVICEGAGS PAEINLRNGD YVNMGLARHA GLPVIVVGDI DRGGVFASMF
GTVALLDPAD QALVAGFVIN KFRGDLGLLQ PGLDMLRQVT GRPTYGVLPW HLDLWLDAED
SLAYGRVLGR PAAPYGDEWL DVAVVRLPRV SNATDVEALA TEPGVRVRLT VEPAELAAAD
LVVLPGSKST VADLAWLRET GLADAVLAHA AAGRPLLGIC GGFQMLGRAI HDPVESRRGS
VPGLGLLPIE ITFDPRKTVR QSAGNAFGGV EVNGYEIHHG YVSAADPELP PLLTYADGRS
EGALLGAVYG THWHGAFESD DFRRRFLAEV ARQAGRHGFR PAPATSFAAA RERSLDLLGD
LVEEHLDTDA LWQLVESGPP TGLPFIPPGA PTR
//
