ID A0A024JXD3_9MYCO Unreviewed; 482 AA.
AC A0A024JXD3;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 57.
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:CDO87913.1};
GN ORFNames=BN973_02271 {ECO:0000313|EMBL:CDO87913.1};
OS Mycobacterium triplex.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium simiae complex.
OX NCBI_TaxID=47839 {ECO:0000313|EMBL:CDO87913.1};
RN [1] {ECO:0000313|EMBL:CDO87913.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO87913.1};
RX PubMed=24874681; DOI=10.1128/genomeA.00499-14;
RA Sassi M., Croce O., Robert C., Raoult D., Drancourt M.;
RT "Draft Genome Sequence of Mycobacterium triplex DSM 44626.";
RL Genome Announc. Announc.2:e00499-e00414(2014).
RN [2] {ECO:0000313|EMBL:CDO87913.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO87913.1};
RA Xu Y.W., Yang Q.;
RL Submitted (APR-2014) 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; HG964446; CDO87913.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024JXD3; -.
DR STRING; 47839.BN973_02271; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_11; -.
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-UniRule.
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; 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}.
FT DOMAIN 2..214
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 242..414
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 321
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 406
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 482 AA; 51362 MW; 82EE0D3D77C82B4E CRC64;
MLVAGLCRLL ARDGVRVAPF KAQNMSNNSA VTVEGGEIGR AQAIQARAAG LEPSVRFNPI
LLKPGSDRTS QLVIRGRVAD SVTAAGYFEH RDRLAKVVAD ELASLRDEFD VVICEGAGSP
AEINLRATDL ANMGLARAAN LPVVLVGDID RGGLLAHLFG TVAVLEARDQ ALIAGFIVNK
FRGDPALLEP GLRQLLELTG RPTYGVVPYA DELWLDAEDS LSALAHSVVG RPAPPRGGEW
LTVAAVRLPR ISNSTDIEAL ACEPGVRVRW ISDPADLADA DLVVIPGSKA TVADLHWLRE
RGLAAAIAEH ATAGKPVLGI CGGLQMLCRR IQDTVESGSG EVAGLGLLDA DIVFGEHKTL
RRWQHPLAGY EIHHGQVIRC GEAAWFDVDA QPHGIARGAV FGTHWHGLLD NDDFRRAWLS
RVAAAAGRTK FVVADDTDVA ARRDAQLDVA AELLASHLDI DAVVGLLDGP PPRPQIASRL
RP
//
