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Database: UniProt
Entry: A0A1K1TGM2_STRAR
LinkDB: A0A1K1TGM2_STRAR
Original site: A0A1K1TGM2_STRAR 
ID   A0A1K1TGM2_STRAR        Unreviewed;       508 AA.
AC   A0A1K1TGM2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN   ORFNames=SAMN02787144_100170 {ECO:0000313|EMBL:SFW99429.1};
OS   Streptomyces atratus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1893 {ECO:0000313|EMBL:SFW99429.1, ECO:0000313|Proteomes:UP000181909};
RN   [1] {ECO:0000313|EMBL:SFW99429.1, ECO:0000313|Proteomes:UP000181909}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK807 {ECO:0000313|EMBL:SFW99429.1,
RC   ECO:0000313|Proteomes:UP000181909};
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}.
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; FPJO01000001; SFW99429.1; -; Genomic_DNA.
DR   RefSeq; WP_072483010.1; NZ_FPJO01000001.1.
DR   AlphaFoldDB; A0A1K1TGM2; -.
DR   STRING; 1893.SAMN02787144_100170; -.
DR   OrthoDB; 9808302at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000181909; 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..235
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          262..432
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        341
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        425
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   508 AA;  54004 MW;  A5BFE7C737BC92B8 CRC64;
     MSGGLLVAGT TSDAGKSVVT AGICRWLVRR GVKVAPFKAQ NMSLNSFVTR EGAEIGRAQA
     MQAQAARVEP SALMNPVLLK PGSDRSSQVV LMGKPVGEMS ARGYHGGRQQ ALLSTVVDCL
     EQLRSTYDAV ICEGAGSPAE INLRRTDIVN MGIARAARFP VVVVGDIDRG GVFASFFGTT
     ALLAAEDQSL IAGYLVNKFR GDVSLLEPGL EMLRDITGRP TYGVLPFAHG LGIDEEDGLR
     VSLRGAVRES VVAPPHGEDV LRVAVCAVPL MSNFTDVDAL AAEPGVVVRF VDRAEELSDA
     DLVVVPGTRG TVKALAWLRE RGLADALARR AAEGRPVLGI CGGFQVLGEH IEDEVESRAG
     RVEGLGLLPV RIRFDREKTL ARPVGEALGA PVEGYEIHHG VADVHGGEPF LDGCRVGVVW
     GTHWHGSLES DEFRRRFLTE VARAAGRRFV PAPDTAFAAL REEQLDRLGD LVEEHADTDA
     LLRLLESGAP SGLPFIAPGA PAATGSRR
//
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