ID A0A1A0TYF3_9MYCO Unreviewed; 503 AA.
AC A0A1A0TYF3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=A5758_22700 {ECO:0000313|EMBL:OBB63817.1};
OS Mycobacterium sp. 852014-50255_SCH5639931.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834112 {ECO:0000313|EMBL:OBB63817.1, ECO:0000313|Proteomes:UP000092113};
RN [1] {ECO:0000313|EMBL:OBB63817.1, ECO:0000313|Proteomes:UP000092113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=852014-50255_SCH5639931 {ECO:0000313|EMBL:OBB63817.1,
RC ECO:0000313|Proteomes:UP000092113};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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}.
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:OBB63817.1}.
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DR EMBL; LZSV01000035; OBB63817.1; -; Genomic_DNA.
DR RefSeq; WP_067744511.1; NZ_LZSV01000035.1.
DR AlphaFoldDB; A0A1A0TYF3; -.
DR STRING; 1834112.A5758_22700; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000092113; 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.
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 6..232
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 259..435
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 338
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 427
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 503 AA; 53133 MW; A2275EAA92DB9533 CRC64;
MSGALLVAGT SSDAGKSVVV AGLCRLLARR GVRVAPFKAQ NMSNNSVVTV EGGEIGRAQA
LQARAAGLAP SVRFNPILLK PGSDRTSQLV IRGQVADSVT AASYVRHRDR LAGIVADELS
CLRDDFDAVI CEGAGSPAEI NLRATDLANM GLARAANLPV ILVGDIDRGG LLAHLFGTVA
VLEPEDQALI AGFVVNKFRG DPALLEPGLR QLHAMTGRPT YGVLPYADEL WLDAEDSLSV
VARRLVGTPE PPRGSEWLRV AAIRLPRISN STDVEALACE PGVAVRWSAD PADLADTDLI
VIPGSKSTVA DLTWLRDHGL AEAITAHAAA GKPVLGICGG FQMLCRRLDD PVESAVGEVA
GLGLLDADIA FGETKILRRW PPPLAGYEIH HGRVSRCAED IWFGAEGGRD CQPHGLARGA
VFGTHWHGLL DNDDFRRAWL TCVAAAAGRD GFVVADTNVA ARRDAQLDVI ADLLADHLDT
DAVLGLLDGP PPRRPHLATR LGP
//
