ID A0A117I544_9MYCO Unreviewed; 499 AA.
AC A0A117I544;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=RMCB_2041 {ECO:0000313|EMBL:GAS87945.1};
OS Mycolicibacterium brisbanense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=146020 {ECO:0000313|EMBL:GAS87945.1, ECO:0000313|Proteomes:UP000069620};
RN [1] {ECO:0000313|EMBL:GAS87945.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM15654 {ECO:0000313|EMBL:GAS87945.1};
RA Katahira K., Ogura Y., Gotoh Y., Hayashi T.;
RT "Draft Genome Sequences of Five Rapidly Growing Mycobacterium Species, M.
RT thermoresistibile, M. fortuitum subsp. acetamidolyticum, M. canariasense,
RT M. brisbanense, and M. novocastrense.";
RL Genome Announc. 4:e00322-16(2016).
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: 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:GAS87945.1}.
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DR EMBL; BCSX01000021; GAS87945.1; -; Genomic_DNA.
DR RefSeq; WP_062828694.1; NZ_JACKTM010000020.1.
DR AlphaFoldDB; A0A117I544; -.
DR STRING; 146020.RMCB_2041; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000069620; 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; 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.
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 7..231
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 260..426
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 339
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 419
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 499 AA; 52519 MW; E1C1B3698DEE30B8 CRC64;
MSGGALLVAG TTSDAGKSMV VAGLCRLLAR RGVRVAPFKA QNMSNNSAVT VDGGEIGRAQ
AMQARAAGLA PHTRFNPILL KPGSDRTSQL VLRGRVAGSV CAGDYFTHRE RLAAVVADEL
SSLRAEFDVV ICEGAGSPAE INLRATDLAN MGLARAAQLP VVLVGDIDRG GLLAHLHGTV
AVLEPADQAL IAGFVVNKFR GDPALLEPGL RQLHALTGRP TYGVIPFHDG IWLDTEDSVS
VRAGGLVGPP QPPRGEQTLT VAAIRLPRIS NSTDVEALAC EPGVDVRWVA DAADLAGADV
VVIPGSKATV SDLAWLTERG LAEAIRTHAA QGRAVLGVCG GFQMLCRRID DSVESRAGSV
AALGLLAADI VFDPEKTLRR WDAPLYGYEI HHGRVVGCEE QDWLGVGVRR GAVYGTHWHG
LLDNDAVRRS WLTEVARAAG RAGFVVADDV DVAARRDAQL DLMADLLAEH LDTDAVMDLL
AHGPPSRPTM RTALDGPTG
//
