ID M1Z9G3_9FIRM Unreviewed; 280 AA.
AC M1Z9G3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028,
GN ECO:0000313|EMBL:SHD77591.1};
GN ORFNames=CUESP1_2237 {ECO:0000313|EMBL:SHD77591.1};
OS [Clostridium] ultunense Esp.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Tepidimicrobiaceae;
OC Schnuerera.
OX NCBI_TaxID=1288971 {ECO:0000313|EMBL:SHD77591.1, ECO:0000313|Proteomes:UP000245423};
RN [1] {ECO:0000313|EMBL:SHD77591.1, ECO:0000313|Proteomes:UP000245423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Clostridium ultunense strain Esp {ECO:0000313|EMBL:SHD77591.1};
RA Manzoor S.;
RL Submitted (NOV-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|HAMAP-Rule:MF_00028}.
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DR EMBL; LT669839; SHD77591.1; -; Genomic_DNA.
DR AlphaFoldDB; M1Z9G3; -.
DR HOGENOM; CLU_019250_0_0_9; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000245423; Chromosome chri.
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-KW.
DR CDD; cd05389; CobQ_N; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00028; CobQ; 1.
DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR InterPro; IPR047045; CobQ_N.
DR InterPro; IPR004459; CobQ_synth.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21343:SF1; COBYRIC ACID SYNTHASE; 1.
DR PANTHER; PTHR21343; DETHIOBIOTIN SYNTHETASE; 1.
DR Pfam; PF01656; CbiA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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:UP000245423}.
FT DOMAIN 4..226
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
SQ SEQUENCE 280 AA; 31459 MW; F207FCF950F82570 CRC64;
MANIMIQGTT SSAGKSFICT ALCRIFKEDG YKVAPFKSQN MSSKFYETEE GYKMSTAQAL
QAKAAGIKPN PNMNPILLIP NSDKGSDVII KGKFYNRMEA LEYFTYKDEL KPMIKEAYKN
LEKENHIMVL EGAGSPAEIN LKENDIVNMG MAKMADAPVL LVADIDRGGV FASLYGTVIL
LEEEERARIK GLIINKFRGD KRLLDPGIEM IEELLNIPVI GTLPLTPLEL VDEDSLIDYE
KHCNLFPQRE DEIEGELGKL SKMVRENLDM DYIYSLLKLD
//
