ID A0A135L5R2_9BACI Unreviewed; 494 AA.
AC A0A135L5R2;
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=U473_10140 {ECO:0000313|EMBL:KXG44326.1};
OS Tepidibacillus decaturensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Tepidibacillus.
OX NCBI_TaxID=1413211 {ECO:0000313|EMBL:KXG44326.1, ECO:0000313|Proteomes:UP000070352};
RN [1] {ECO:0000313|EMBL:KXG44326.1, ECO:0000313|Proteomes:UP000070352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z9 {ECO:0000313|EMBL:KXG44326.1,
RC ECO:0000313|Proteomes:UP000070352};
RA Dong Y., Chang J.Y., Sanford R., Fouke B.W.;
RT "Draft Genome for Tepidibacillus decaturensis nov. sp. Strain Z9, an
RT Anaerobic, Moderately Thermophilic and Heterotrophic Bacterium from Deep
RT Subsurface of the Illinois Basin, USA.";
RL Submitted (FEB-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|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:KXG44326.1}.
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DR EMBL; LSKU01000001; KXG44326.1; -; Genomic_DNA.
DR RefSeq; WP_068725928.1; NZ_LSKU01000001.1.
DR AlphaFoldDB; A0A135L5R2; -.
DR STRING; 1413211.U473_10140; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000070352; 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; 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; PF13500; AAA_26; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000070352}.
FT DOMAIN 254..438
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 333
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 431
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 494 AA; 56866 MW; 462DDFE4EC96ABE9 CRC64;
MAKALMIVGT GSDVGKSRIV TALCRYFSQR NVSVAPFKAQ NMALNSYITV DGKEIGRAQG
LQADAAGIVA SEHMNPILLK PSNPYASQVI VHGKPIAQMN FRDYRETKHE ELKKIVQDSL
AKLQAEYDLI LIEGAGSPVE MNLKDRDIVN MKVAEWANAD VILVADIDRG GVFAQIVGTL
QLLTEEERKR VKGIFINKFR GDLQLFQSGI EWIEKYTDIP VLAVFPFYPL PEWEEEDSVA
LQQKQKVKEN ADLDIVVVKY PYISNYTDFI PLELEEDVQI RYVNNVKEFG NPHVVILPGT
KNTMEDLQFL QQSGFWQKIV DHVAQQRELV GICGGYQMLG ERLLDPDLIE SNVLSREGFA
FFPMVTRFEK EKKTVRVKGK KVHSKLPILG YEIHMGMVEW TEKQEGMFLL ENGTLEGFHH
PNLPAWGTFI HGIFDSDHFR HEWLERLREK YGLPPRKDRV AFSRRKEKMF ENLEDWFIHS
LRPVYVQFFD HYIF
//
