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Database: UniProt
Entry: A0A0B3SI32_9RHOB
LinkDB: A0A0B3SI32_9RHOB
Original site: A0A0B3SI32_9RHOB 
ID   A0A0B3SI32_9RHOB        Unreviewed;       481 AA.
AC   A0A0B3SI32;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Cobyric acid synthase {ECO:0000256|ARBA:ARBA00019833, ECO:0000256|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028,
GN   ECO:0000313|EMBL:KHQ50244.1};
GN   ORFNames=OA50_05240 {ECO:0000313|EMBL:KHQ50244.1};
OS   Mameliella alba.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Mameliella.
OX   NCBI_TaxID=561184 {ECO:0000313|EMBL:KHQ50244.1, ECO:0000313|Proteomes:UP000030960};
RN   [1] {ECO:0000313|EMBL:KHQ50244.1, ECO:0000313|Proteomes:UP000030960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMTAT08 {ECO:0000313|EMBL:KHQ50244.1,
RC   ECO:0000313|Proteomes:UP000030960};
RA   Gan H.Y., Muhd D.-D., Mohd Noor M.E., Yeong Y.S., Usup G.;
RT   "Genome sequence of Ponticoccus sp. strain UMTAT08 isolated from clonal
RT   culture of toxic dinoflagellate Alexandrium tamiyavanichii.";
RL   Submitted (OCT-2014) 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|ARBA:ARBA00025166, 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|ARBA:ARBA00006205, ECO:0000256|HAMAP-Rule:MF_00028}.
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:KHQ50244.1}.
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DR   EMBL; JSUQ01000029; KHQ50244.1; -; Genomic_DNA.
DR   RefSeq; WP_043146490.1; NZ_JSUQ01000029.1.
DR   AlphaFoldDB; A0A0B3SI32; -.
DR   STRING; 561184.SAMN05216376_11620; -.
DR   PATRIC; fig|1515334.3.peg.5257; -.
DR   OrthoDB; 9808302at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000030960; 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:UP000030960}.
FT   DOMAIN          5..237
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          252..435
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        331
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        428
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   481 AA;  51439 MW;  90E67FE0F5680DF9 CRC64;
     MSRAVMIQGT GSNVGKSMLV AGLCRAARRR GLSVAPFKPQ NMSNNAAVTS DGGEIGRAQA
     LQALACGLPL HTDMNPVLLK PETDVGAQVV VQGKRLTTAK ARDYAKLKPQ LLGSVIESFN
     RLRSAHDLVI VEGAGSPAEV NLRKGDIANM GFAEAAGVPV ILAGDIDRGG VIAQIVGTQA
     ILSTDDANHI SGFLINKFRG DPRLFDEGYK LIEERTGWRG YGVAPWFPGA WRLPAEDALD
     IRTQTRAEGL HVVCLCLSRM ANFDDLDPLA QEPDVRLTML RRGEAIPGDA DLVILPGSKS
     TRGDLAFLRE QGWDVDLMAH HRRGGRVLGI CGGYQMLGRV VDDPQGIEGP AGRDPGLGLL
     EIDTVMTADK SLTEVNARHA ATGTTFHGYE IHIGRSEGPD RARPFAFVGD NPEGAISADG
     RVMGSYLHGM FRDDRFRAAW LEGFGVAASA SYDATVEQTL EALADHLEAH LDVEGILAAA
     R
//
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