ID   A0A1G8HID6_9PSED        Unreviewed;       483 AA.
AC   A0A1G8HID6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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   ORFNames=SAMN05216603_12035 {ECO:0000313|EMBL:SDI06389.1};
OS   Pseudomonas benzenivorans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=556533 {ECO:0000313|EMBL:SDI06389.1, ECO:0000313|Proteomes:UP000199168};
RN   [1] {ECO:0000313|Proteomes:UP000199168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8628 {ECO:0000313|Proteomes:UP000199168};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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|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}.
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DR   EMBL; FNCT01000020; SDI06389.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8HID6; -.
DR   STRING; 556533.SAMN05216603_12035; -.
DR   OrthoDB; 9808302at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000199168; 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}.
FT   DOMAIN          4..229
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          250..434
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        329
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        427
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   483 AA;  51345 MW;  AB8F0E11F2B46F10 CRC64;
     MTTLMVQGTT SDAGKSTLVT ALCRWLKRQG VAVAPFKPQN MALNSAVTAD GGEIGRAQAV
     QAQAAGLAPH SDMNPVLLKP NSDTGAQVII HGRAISSMEA AAYHDYKQVA MQAVLASHRR
     LCATYPLLLV EGAGSPAEIN LRAGDIANMG FAEAVDCPVI LIADIDKGGV FAHLVGTLAL
     LSESEQARVC GFVINRFRGD IGLLQPGLDW LERRTGKPVL GVLPYLMDFH LEAEDAIDVR
     QSAKAAEALR VVVPVLPRIS NHTDFDPLRL HPQVELSFVG PGQPIPPADL IVLPGSKSVR
     ADLAYLRAQG WDAAIHKHLR YGGKLLGICG GLQMLGRLID DPHGLEGAPG SSPGLGLLEF
     ATVLEPEKQL RNVRGRLCLE GAPVCGYEIH AGVSSGPALE VAAVQLDDGR GDGALSADGQ
     VLGTYLHGLF ESSAACSALL RWAGLRAVQQ VDYQALRERD IERLADMVEA HLDTDRLRQL
     CGL
//