ID A0A428X8N3_9ACTN Unreviewed; 518 AA.
AC A0A428X8N3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=DMB66_41520 {ECO:0000313|EMBL:RSM51664.1};
OS Actinoplanes sp. ATCC 53533.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1288362 {ECO:0000313|EMBL:RSM51664.1, ECO:0000313|Proteomes:UP000287606};
RN [1] {ECO:0000313|EMBL:RSM51664.1, ECO:0000313|Proteomes:UP000287606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53533 {ECO:0000313|EMBL:RSM51664.1,
RC ECO:0000313|Proteomes:UP000287606};
RA Waglechner N., Wright G.D.;
RT "Evolution of GPA BGCs.";
RL Submitted (MAY-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:RSM51664.1}.
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DR EMBL; QHHV01000155; RSM51664.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428X8N3; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000287606; 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:UP000287606}.
FT DOMAIN 6..235
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 261..440
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 432
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 518 AA; 54373 MW; 6CC35690042E629F CRC64;
MNGGLLVAGT TSDAGKSVLT AGICRWLHRR GVKVAPFKAQ NMSNNSVVVV GADGRGGEIG
RAQAMQAAAC GIAPDIRFNP VLLKPGSDFS SQVVLLGQAI DTVTAGNYRS LRPRLAETAH
ATLAELRAEY DAVICEGAGS PAEINLRDGD FVNMGLARHA GLPAIVVGDI DRGGVFAALF
GTVALLSPED QALISGFVIN KFRGDLGLLR PGLDMITAAT GRPVHGVLPF DLDVWLDAED
SLAYGRVLGR PAAPRGTEWL RVAVVRLPRI SNATDAEALA TEPGVRVRLT IEPAEIADAD
LVVLPGSKAT VSDLAWLRET GLADAVRAHA AAGKPLVGIC GGFQMLADTI HDDVESRRGT
VAGLGLLPVE VTFGARKTLA RSRGAAWEQV PVSGYEIHHG YVSAGEPAPL LRYADGAPEG
AVVGAVSGTH WHGAFESDEF RRRFLTEAAR QAGRHGFEVA PDTRFAEVRE RALDVLGDLV
EEHLDTDALW RLIESGPSTG LPFIPPGAPA QPGAADGR
//
