COBQ_GEOSW
ID COBQ_GEOSW Reviewed; 503 AA.
AC C5DAP4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=GWCH70_1560;
OS Geobacillus sp. (strain WCH70).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC unclassified Geobacillus.
OX NCBI_TaxID=471223;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCH70;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brumm P., Mead D.A., Richardson P.;
RT "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL Submitted (JUN-2009) 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:0000255|HAMAP-Rule:MF_00028}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
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DR EMBL; CP001638; ACS24358.1; -; Genomic_DNA.
DR RefSeq; WP_015863816.1; NC_012793.1.
DR AlphaFoldDB; C5DAP4; -.
DR SMR; C5DAP4; -.
DR STRING; 471223.GWCH70_1560; -.
DR EnsemblBacteria; ACS24358; ACS24358; GWCH70_1560.
DR KEGG; gwc:GWCH70_1560; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_9; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
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; cd01750; GATase1_CobQ; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 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; IPR004459; CobQ_synth.
DR InterPro; IPR011698; GATase_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21343:SF1; PTHR21343:SF1; 1.
DR Pfam; PF01656; CbiA; 1.
DR Pfam; PF07685; GATase_3; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00313; cobQ; 1.
DR PROSITE; PS51274; GATASE_COBBQ; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Glutamine amidotransferase.
FT CHAIN 1..503
FT /note="Cobyric acid synthase"
FT /id="PRO_1000201968"
FT DOMAIN 255..444
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 337
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 436
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 503 AA; 56403 MW; 20D93915BCC679F0 CRC64;
MAKALPIMFQ GTHSDAGKSI IATAFCRIFA KNGWKTAPFK SQNMSLNSYV TVDGKEIGRA
QGIQAEAAGV VATTDMNPIL IKPSREHESQ IVVHGKPYKN MQAFAYRGEF FEKGLAIIHE
SLDVLMNEYD RLVIEGAGSP AEINLNDREL VNMRVARMAN APVVLIGDIE RGGVFASLVG
TLQLLDKEDR KRIIGVIINK FRGDLALLKP GLDWFEQYTG VPVLGVVPYL EDLHIDAEDS
VSLEQMSTAV NPDKDIDIAV IRYPKISNFT DVDPFLTEPD CHVRFVATAA QLGQPDLLIL
PGSKNTIEDL LYMKKNGIAE QIAQLNKHHR VTIVGICGGY QMLGARIRDP FGVETPLREI
SGLNLLPIET TLERKKTTVL SEGILTFTGE RFFVKGYEIH MGRSQPLDGN IPFIHVQGRA
EGAKSKDERV IGTYFHDLFH NDAFREALLN KIRREKGLAP IYGRQSFRTI REQAFDRLAD
HVKRHVCIEE IEEKMYMFQR RDV