ID A0A2S9KBB4_9BURK Unreviewed; 494 AA.
AC A0A2S9KBB4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|ARBA:ARBA00019833, ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=C6P61_14770 {ECO:0000313|EMBL:PRD67759.1};
OS Malikia spinosa.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Malikia.
OX NCBI_TaxID=86180 {ECO:0000313|EMBL:PRD67759.1, ECO:0000313|Proteomes:UP000238326};
RN [1] {ECO:0000313|EMBL:PRD67759.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=83 {ECO:0000313|EMBL:PRD67759.1};
RA Suzuki S., Ishii S., Walworth N., Bird L., Kuenen J.G., Nealson K.H.;
RT "Comparative genomics illustrates the genes involved in a hyperalkaliphilic
RT mechanisms of Serpentinomonas isolated from highly-alkaline calcium-rich
RT serpentinized springs.";
RL Submitted (MAR-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|ARBA:ARBA00025166, 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|ARBA:ARBA00006205, 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:PRD67759.1}.
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DR EMBL; PVLR01000046; PRD67759.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S9KBB4; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000238326; 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 15..238
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 265..455
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 344
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 449
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 494 AA; 52596 MW; 7CE6937F15C5EE70 CRC64;
MNLQANSGPQ RAKCVMVLGT SSGAGKSWLA TALCRHYARQ GLKVAPFKAQ NMSNNARVVA
SPGGSGEIGS AQYFQALAAR AEPDVRMNPL LLKPEADTRS QVVMLGQVDA ELSTMPWRGR
SEKVWPRIAQ ALDDLRAEYD VVVIEGAGSP AEINLMASDI VNLRVARAAD ARCLLVTDID
RGGAFAHLYG TWALLPEADR ARIDGFVLNK FRGDATLLAP APEQLEQLTG VPTVATLPMW
WQHGLPEEDG VFDDRSRSQG AVTRTVAVVA YPRLSNLDEF QPLKNIPGLR LVWARSPAEL
AGADWIVLPG SKHTSSDLAW LREQGLDRAI TDHAGQGGAV LGICGGLQML GEALIDTHGV
DGNAPGLGLL PLVTQFDPDK TVQRTQAGFG DLVGAWSALS GVAVQGYEIH HGQTAQHPAM
AAAGDIAREV LPGLAWQNER GNVLGCYLHG LFEDPAVLQA LFGASAPTLD CVFDGLADYL
EQHIAPGLLD ALIA
//
