ID   A0A286GHX8_9PROT        Unreviewed;       490 AA.
AC   A0A286GHX8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=SAMN05421508_104220 {ECO:0000313|EMBL:SOD95082.1};
OS   Caenispirillum bisanense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Novispirillaceae; Caenispirillum.
OX   NCBI_TaxID=414052 {ECO:0000313|EMBL:SOD95082.1, ECO:0000313|Proteomes:UP000219621};
RN   [1] {ECO:0000313|EMBL:SOD95082.1, ECO:0000313|Proteomes:UP000219621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USBA 140 {ECO:0000313|EMBL:SOD95082.1,
RC   ECO:0000313|Proteomes:UP000219621};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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; OCNJ01000004; SOD95082.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286GHX8; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000219621; 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:UP000219621}.
FT   DOMAIN          10..242
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          261..445
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        438
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   490 AA;  50934 MW;  4485B94EACEF1D96 CRC64;
     MSGGTRTPAL MFQGTGSDVG KSLLVAGFCR LFTRRGLRVR PFKPQNMSNN AAVTPDGGEI
     GRAQALQARA CGIATSRHMN PVLLKPQTDV GAQVVVQGTV LANAGARDYF RLKPSLLPKV
     LESYAALAAE ADLVLVEGAG SAAEVNLRAA DIANMGFAEA ADLPVVLVGD IDRGGVLAQI
     VGTHALLPAA ERARVVGYLV NKFRGDPSLF TPALDIIGGH TGWPSLGVLP WFARAADLPA
     EDAMALDQRR DGPAGGEGRV KVAVLRLSRI ANFDDFDPLA AEPEVALTWV QPGRAIPGDA
     DVVILPGSKA TLADLAFLRA QGWDVDLAAH LRRGGRVIGI CAGYQMLGRV VRDPEGIEGP
     PGEAAGLGLL DVETVMRGPK TLREAAGTEV GSGLAVAGYE MHMGKTAGPD RDRPWLHLGD
     GPDGAVSADG RVRGCYLHGL FAADAFRRAV LGLDGAPVAY EAGVDAALDA LADHLEAHAD
     LPALERAAGL
//