ID A0A367F8R3_9ACTN Unreviewed; 523 AA.
AC A0A367F8R3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=DTL70_06200 {ECO:0000313|EMBL:RCG26651.1};
OS Streptomyces diacarni.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2800381 {ECO:0000313|EMBL:RCG26651.1, ECO:0000313|Proteomes:UP000252914};
RN [1] {ECO:0000313|EMBL:RCG26651.1, ECO:0000313|Proteomes:UP000252914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LHW51701 {ECO:0000313|EMBL:RCG26651.1,
RC ECO:0000313|Proteomes:UP000252914};
RA Li L.;
RT "Streptomyces reniochalinae sp. nov. and Streptomyces diacarnus sp. nov.
RT from marine sponges.";
RL Submitted (JUN-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:RCG26651.1}.
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DR EMBL; QOIN01000033; RCG26651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367F8R3; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000252914; 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:UP000252914}.
FT DOMAIN 8..251
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 275..452
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 354
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 446
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 523 AA; 55126 MW; E1F7168705ABBD54 CRC64;
MSGGGGLLVA GTTSDAGKSV VTAGICRWLT RKGLRVAPFK AQNMSLNSYV TLDGAEIGRA
QAMQAAAART EPSALMNPVL LKPGGDRTSQ VVLLGKPVGE MSAQGYFGRR TGEGQGVRFG
RREELLETVA GCLEELRRTH DAVVCEGAGS PAEINLRRSD IVNMGLARAC RLPVVVVGDI
DRGGVFASLF GTTALLAPED QELVAGYLVN KFRGDVSLLE PGLEMLRGLT GRPTLGVLPF
RHGLGIDEED GLRVSLRGAV RDSSVAAPHG ADVLRVAVLA VPLMSNFTDV DALAAEPGVV
VRFCDRAEEL ADADLVVVPG TRGTVGALEW LRERGLADAV ARRAAEGRPV LGICGGYQLL
GERIEDEVES RAGLVDGLGL LPVRVRFAHG KTLARPHGTA LGEPVEGYEI HHGVAEVHGG
EGFFRSAGGG ELDGCRVGAV WGTHWHGSLE SDGFRRAFLR RVAADAGRAF EPAPDTRFAA
LREEQLDLLG DLIEEHADTA ALLRLIEEGV PEGLPFVPPG APP
//
