ID A0A0K1JMI8_9MICO Unreviewed; 498 AA.
AC A0A0K1JMI8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=VV02_21260 {ECO:0000313|EMBL:AKU17790.1};
OS Luteipulveratus mongoliensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Luteipulveratus.
OX NCBI_TaxID=571913 {ECO:0000313|EMBL:AKU17790.1, ECO:0000313|Proteomes:UP000066480};
RN [1] {ECO:0000313|EMBL:AKU17790.1, ECO:0000313|Proteomes:UP000066480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MN07-A0370 {ECO:0000313|EMBL:AKU17790.1,
RC ECO:0000313|Proteomes:UP000066480};
RA Juboi H., Basik A., Shamsul S.S., Arnold P., Schmitt E.K., Sanglier J.-J.,
RA Yeo T.;
RT "Luteipulveratus halotolerans sp. nov., a novel actinobacterium
RT (Dermacoccaceae) from Sarawak, Malaysia.";
RL Submitted (MAR-2015) 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; CP011112; AKU17790.1; -; Genomic_DNA.
DR RefSeq; WP_052594811.1; NZ_CP011112.1.
DR AlphaFoldDB; A0A0K1JMI8; -.
DR STRING; 571913.VV02_21260; -.
DR KEGG; lmoi:VV02_21260; -.
DR PATRIC; fig|571913.6.peg.4311; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000066480; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000066480}.
FT DOMAIN 6..230
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 254..426
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 333
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 421
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 498 AA; 53119 MW; DA51843E3EF6119D CRC64;
MPGSLLVAGT TSDAGKSVVT AGVCRLLARE GLSVAPFKAQ NMSNNSMVTA AGAEIGRAQW
VQAVAAGAEP EPAMNPVLLK PSSDRRSHVV VMGQPAGRLE AGEYAGGRAH LAEAAFAAYD
DLRSRFDVVV CEGAGGVAEI NLREWDYVNL GLAQHDSMPT LLVADIDRGG VFAQLYGSVA
LLDERDQALV AGFVINKFRG DVSLLAPGTT ELERLTGRPV LGILPWQHGL WLDSEDAVAI
DQRPLPRDAA HALRVAVLAF PRISNFTDID ALSLEPDVDV RFVSRPEDVT AADLVVLPGT
RSTLGDLAWM RDRGLDEAVR RHAASGLPVL GICGGCQMLG QEIVDPDGVE GPAGATVPGL
GLLEMRTTFE RDKALALVEG EWSGEKVSGY VIHHGRITLG DNATPFLDGM EQDAVRGTMW
HGSLESDGFR RRLLSNAARS AGRTSFRPDP DLSFTDARMS RLDLLADLLE EHIGVDPLLR
LIEQGTPRGL PFIAAGPR
//
