ID A0A1M6LB36_9ACTN Unreviewed; 480 AA.
AC A0A1M6LB36;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=SAMN02745244_03033 {ECO:0000313|EMBL:SHJ68417.1};
OS Tessaracoccus bendigoensis DSM 12906.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=1123357 {ECO:0000313|EMBL:SHJ68417.1, ECO:0000313|Proteomes:UP000184512};
RN [1] {ECO:0000313|EMBL:SHJ68417.1, ECO:0000313|Proteomes:UP000184512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12906 {ECO:0000313|EMBL:SHJ68417.1,
RC ECO:0000313|Proteomes:UP000184512};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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DR EMBL; FQZG01000069; SHJ68417.1; -; Genomic_DNA.
DR RefSeq; WP_073189824.1; NZ_FQZG01000069.1.
DR AlphaFoldDB; A0A1M6LB36; -.
DR STRING; 1123357.SAMN02745244_03033; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000184512; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000184512}.
FT DOMAIN 5..229
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 255..422
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 334
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 418
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 480 AA; 51325 MW; E5DB9AF7371D6B22 CRC64;
MTGLLIAGTS SDAGKSLFVT GLCRVARRRG IDVAPFKAQN MSNNSMVCLD GSEIGRAQYL
QAIAAGVAPE AVLNPVLLKP GTDRRSFVVL RGQPYGTLEA GEYTTGRRHL AESAFSAYEE
LAATHELVIC EGAGSPAEIN LRVGDYTNMG LARRFDLPVA LIGDIDRGGV LASIFGTWGL
LDDADRALLR GYIINKFRGD QAILEPGLEE ITARTGLTDF GVLPWLNGVW IDGEDALEVG
RWRNDGGASD PGDLRVAVVR LPRISNATDV DALAQEPGVT VEVTLDPRVV EEADLAVLPG
TRATLDDLAW LRETGIAEAV ARRAEAGRAV LGICGGFQML ARTIDDDVEG SGVATGLGLL
PVDIEFHAEK VLGRPVGNWR GHPVDGYTIH HGRPTVDPGV EHFLEGAHVG AVWGTMWHGS
LECDDFRRAW LTAVASQAGS SWLPRSGGTG FGALREQMIE TTADAIEEHI RVDELLNLAR
//
