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Database: UniProt
Entry: G2GET4_9ACTN
LinkDB: G2GET4_9ACTN
Original site: G2GET4_9ACTN 
ID   G2GET4_9ACTN            Unreviewed;       502 AA.
AC   G2GET4;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN   ORFNames=SZN_20087 {ECO:0000313|EMBL:EGX57995.1};
OS   Streptomyces zinciresistens K42.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=700597 {ECO:0000313|EMBL:EGX57995.1, ECO:0000313|Proteomes:UP000004217};
RN   [1] {ECO:0000313|EMBL:EGX57995.1, ECO:0000313|Proteomes:UP000004217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K42 {ECO:0000313|EMBL:EGX57995.1,
RC   ECO:0000313|Proteomes:UP000004217};
RA   Lin Y., Hao X., Johnstone L., Miller S.J., Wei G., Rensing C.;
RL   Submitted (AUG-2011) 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:EGX57995.1}.
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DR   EMBL; AGBF01000071; EGX57995.1; -; Genomic_DNA.
DR   RefSeq; WP_007497812.1; NZ_AGBF01000071.1.
DR   AlphaFoldDB; G2GET4; -.
DR   PATRIC; fig|700597.3.peg.3937; -.
DR   OrthoDB; 9808302at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000004217; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004217}.
FT   DOMAIN          6..238
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          262..431
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   502 AA;  53718 MW;  E30D40F38854AADB CRC64;
     MSGGLLVAGT TSDAGKSVVT AGICRWLVRQ GVKVAPFKAQ NMSLNSFVTR EGAEIGRAQA
     MQAQACRVEP TALMNPVLLK PGGERSSQVV LLGKPVGEMS ARGYHGGRQE RLLGTVLDCL
     TELRSTYDAV ICEGAGSPAE INLRRTDIVN MGVARNARLP VLVVGDIDRG GVFASFFGTV
     ALLSAEDQEL VAGFLVNKFR GDAGLLEPGL DMLHGLTGRR TYGVLPFRHG LGIDEEDGLR
     VSLRGTVREL AVAPPVGEDV LRVAVCAVPL MSNFTDVDAL AAEPGVVVRF ADRPEELADA
     DLVIVPGTRG TVRALDWLRE RGLASALARR AAEERPVLGI CGGFQLLGER IEDDVESRRG
     RVDGLGLLPV RVRFAREKTL TRPVGEALGE RVEGYEIHHG VAEVTGGEPF LDGCRVGRTW
     GTHWHGSLES DGFRRAFLRE VAAAAGRRFV PDPGTSFAAL REEQLDRLGD LIEQHADTDA
     LWRLIESGAP QGLPFIPPGA PA
//
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