ID   A0A1H7SCS9_9BURK        Unreviewed;       505 AA.
AC   A0A1H7SCS9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=SAMN05216359_11464 {ECO:0000313|EMBL:SEL70451.1};
OS   Roseateles sp. YR242.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Roseateles.
OX   NCBI_TaxID=1855305 {ECO:0000313|EMBL:SEL70451.1, ECO:0000313|Proteomes:UP000198631};
RN   [1] {ECO:0000313|EMBL:SEL70451.1, ECO:0000313|Proteomes:UP000198631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR242 {ECO:0000313|EMBL:SEL70451.1,
RC   ECO:0000313|Proteomes:UP000198631};
RA   de Groot N.N.;
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; FOAV01000014; SEL70451.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7SCS9; -.
DR   STRING; 1855305.SAMN05216359_11464; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000198631; 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; 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; 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          14..238
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          264..454
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        343
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        448
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   505 AA;  54289 MW;  EA586ED2CA7E95B9 CRC64;
     MTDKTPGARR GRAVMVLGTT SGAGKSFLTT ALCRWYARQG LRVVPFKAQN MSNNARVVPG
     VGGRMGEIGS AQYFQALAAR ARPEVRMNPV LLKPEKDTAS QVVVLGEVDE ALTRAPWRAR
     SEALWASARM ALHALLDEND VVVIEGAGSP AEINLHASDY VNMRTACEAD AACLLVSDID
     RGGAFAHLFG THQLLPEHER ALIRGFVLNR FRGDAALLAP GPDMLQALTG VPTMATLPMW
     RGHGLPEEDG VFDDRSTGTA GACRVAVVAY PRLSNLDEFQ PLRQLDGVRL SWARTPADLV
     DVDWIILPGS KAVAADLAWL RAQRLDQAIT DHAAAGGRVL GICGGLQMLG EALIDPHGLD
     GNAPGLGLLP LVTQFEREKL LRETEARFAA RLDAPWSALG GQPAHGYEIH HGRTAQHPSL
     AAATPVLFDD RGNTIGWQHG PVLGHYAHGL FEDERVLTAL FQRPVRPLEQ VFNELADYVD
     RHFAPGVLAG LLLPRGAAPP AAVPP
//