COBQ_MYCGI
ID COBQ_MYCGI Reviewed; 491 AA.
AC A4T0R6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Mflv_0360;
OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS PYR-GCK)).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
RL Submitted (APR-2007) 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; CP000656; ABP42854.1; -; Genomic_DNA.
DR RefSeq; WP_011891361.1; NC_009338.1.
DR AlphaFoldDB; A4T0R6; -.
DR SMR; A4T0R6; -.
DR STRING; 350054.Mflv_0360; -.
DR EnsemblBacteria; ABP42854; ABP42854; Mflv_0360.
DR KEGG; mgi:Mflv_0360; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_1_11; -.
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..491
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332349"
FT DOMAIN 253..429
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 334
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 421
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 491 AA; 51878 MW; DAB07868E2AAA866 CRC64;
MTGLLVAGTT SDAGKTAVTT GLCRALARRG VKVAPYKAQN MSNNSMVCTS VDGAGAEIGR
AQWVQALAAR ATPEPAMNPV LLKPGSDRRS HVVLMGRPWG QVSSSDWLEG RRALATAAHE
AFDELASRYE VVVAEGAGSP TEINLRAGDY VNLGLARHAG LPTVVVGDID RGGVFAAFFG
TVALLSPQDQ ALIAGFVVNK FRGDVDLLAP GLRDLERLTG RRVYGTLPWH PDIWLDSEDA
LELAGRRSAQ SGARRVAVIR LPRISNFTDV DALGLEPDLD VVFASHPGSL ADADLVVLPG
TRATIADLAW LRSRGLDSAL RRHVAAGRPV LGICGGFQML GRVIRDPHGV EGPVAGVDGL
GLLDVETTFG PDKVLRLPSG RWFGAPATGY EIHHGRITRG DGVDEFLDGA RCGQVFGTMW
HGALEGDELR SRFLQEALGV APSGVSFPAA REARLDLLGD LVERHLDVDA LLDLAKTGPV
AGLPFLPPGA P