ID A0A150MNZ1_9BACI Unreviewed; 503 AA.
AC A0A150MNZ1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=B4110_1760 {ECO:0000313|EMBL:KYD26180.1};
OS Parageobacillus toebii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Parageobacillus.
OX NCBI_TaxID=153151 {ECO:0000313|EMBL:KYD26180.1, ECO:0000313|Proteomes:UP000075324};
RN [1] {ECO:0000313|EMBL:KYD26180.1, ECO:0000313|Proteomes:UP000075324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4110 {ECO:0000313|EMBL:KYD26180.1,
RC ECO:0000313|Proteomes:UP000075324};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated from
RT Foods.";
RL Submitted (JAN-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: 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:KYD26180.1}.
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DR EMBL; LQYW01000128; KYD26180.1; -; Genomic_DNA.
DR RefSeq; WP_062678667.1; NZ_LQYW01000128.1.
DR AlphaFoldDB; A0A150MNZ1; -.
DR PATRIC; fig|153151.4.peg.831; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000075324; 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}.
FT DOMAIN 7..234
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 257..443
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 337
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 436
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 503 AA; 56334 MW; 42761D9697EE69BB CRC64;
MAKALPIMFQ GTHSDAGKSI IATAFCRIFA QNGWKTAPFK SQNMSLNSYV TVDGKEIGRA
QGIQAEAAGV VATTDMNPIL IKPSREHESQ IVVHGKPYKN MQAFAYRGEF FEKGLAIIRE
SLDVLMNEYD RLVIEGAGSP AEINLNDREL VNMRVARMAN APVVLIGDIE RGGVFASLVG
TLQLLDKEDR KRIIGVIINK FRGDLALLKP GLDWFEQYTG VPVLGVVPYL EDLHIDAEDS
VSLEQMSTAV NPDKDIDIAV IRYPKISNFT DVDPFLTEPD CHVRFVTTAS QLGQPDLLIL
PGSKNTIEDL LYMKKNGIAE QIAQLNKHHR VTIVGICGGY QMLGARIRDP FGVETPLREI
SGLNLLPIET TLERKKTTVL SEGILTFAGE RFFVKGYEIH MGRSQPLDGN IPFIHVQGRA
EGAKSKDERV IGTYFHDLFH NDAFREALLN KIRREKGLAP IYGRQSFRTI REQAFDRLAD
HVKRHVRIEE IEEKMHVFRK GDV
//
