ID I4BCX0_MYCCN Unreviewed; 501 AA.
AC I4BCX0;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
DE Flags: Precursor;
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN OrderedLocusNames=Mycch_0302 {ECO:0000313|EMBL:AFM15127.1};
OS Mycolicibacterium chubuense (strain NBB4) (Mycobacterium chubuense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=710421 {ECO:0000313|EMBL:AFM15127.1, ECO:0000313|Proteomes:UP000006057};
RN [1] {ECO:0000313|EMBL:AFM15127.1, ECO:0000313|Proteomes:UP000006057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBB4 {ECO:0000313|EMBL:AFM15127.1,
RC ECO:0000313|Proteomes:UP000006057};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T.,
RA Holmes A., Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium chubuense NBB4.";
RL Submitted (JUN-2012) 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|PROSITE-ProRule:PRU00605}.
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DR EMBL; CP003053; AFM15127.1; -; Genomic_DNA.
DR RefSeq; WP_014813619.1; NC_018027.1.
DR AlphaFoldDB; I4BCX0; -.
DR STRING; 710421.Mycch_0302; -.
DR KEGG; mcb:Mycch_0302; -.
DR PATRIC; fig|710421.3.peg.293; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_11; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000006057; Chromosome.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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.
DR PROSITE; PS51273; GATASE_TYPE_1; 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}; Ligase {ECO:0000313|EMBL:AFM15127.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006057}.
FT DOMAIN 5..244
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 265..437
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 431
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 501 AA; 52395 MW; 7454D73D4F301940 CRC64;
MAGLLVAGTT SDAGKSLVTT GLCRALARRG VKVAPYKAQN MSNNSMVCAG PSVASEATGD
GSGHGVEIGR AQWVQALAAR AVPEAAMNPV LLKPGSDHRS HVVLMGRPWG EVSSADWLEG
RRALGEAAHA AYDDLASRFD VVIAEGAGSP AEINLRAGDY VNLGLARHAN LPAVVVGDID
RGGVFAAFFG TVALLSPDDQ ALVAGFVVNK FRGDVGLLAP GLRDLERVTG RRVFGTLPWR
SDVWLDSEDA LDLFGRVSSR PGARRVAVIR LPRISNFTDV DALGLEPDLD VVFASQAGAL
ADAELIVLPG TRSTIADLAW LRSRGLDRAI VAHAAAGRPV LGICGGFQML GRTVRDPAGI
EGAATEVAGL GLLDIETNFV AQKALRLPTG SWLGAQAAGY EIHHGRISVG AGVDEFLGGA
RAGSVFGTMW HGAFEGDELR VRFLREALGL EPSGVSFPRA RDERLDLLGD LVEQHLDVEA
LLALIGQGPP RGLPFLPPGA P
//
