ID   A0A330L2W6_9BACT        Unreviewed;       516 AA.
AC   A0A330L2W6;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028,
GN   ECO:0000313|EMBL:SPP63984.1};
GN   ORFNames=NITLEN_11070 {ECO:0000313|EMBL:SPP63984.1};
OS   Nitrospira lenta.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Nitrospira.
OX   NCBI_TaxID=1436998 {ECO:0000313|EMBL:SPP63984.1, ECO:0000313|Proteomes:UP000248168};
RN   [1] {ECO:0000313|Proteomes:UP000248168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lucker S., Sakoula D.;
RL   Submitted (APR-2018) 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}.
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DR   EMBL; OUNR01000001; SPP63984.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A330L2W6; -.
DR   InParanoid; A0A330L2W6; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000248168; 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:UP000248168}.
FT   DOMAIN          8..238
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          258..456
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        337
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        450
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   516 AA;  56088 MW;  BF0380FB202877FA CRC64;
     MSGLAPTIMV QGTASSAGKS LLVTALCRFF RREGLRVAPF KSQNMSLNSA VTIDGLEIGR
     AQAVQAEASG ILSCVDMNPI LLKPEGDRRS QVVVLGKSIG SMLATEYHEY KPRLTTVIAE
     SLTRLRSNYD LVVIEGAGSP AEINLKDRDI VNMHVAKLAD APVILVGDID RGGVFASFVG
     TMELLEPDER DRIAAFVVNK FRGDLALLTP GLEFLSERTG KPVLGVVPYI KDLRIADEDS
     VSLEARLARR RPSQQELDVV VVRVPHLSNY DDVEALEHEA GVVVRFVEQP DEVAGADLVI
     LPGSKSTVAD LAWLRASGFA GAIEARAREG GPLLGVCGGC QMLGEMIDDP HGVESAEPHV
     RGLGLLALRT HFEQEKVTAQ VLARVRCPSF LTDGVGLEEA VHGYEIHMGM VVPHNQQASP
     FEIQSRNGRT KVRSDGALSS DGMVVGTMLH GLFENEVIRA RTLSFLRRRK GIFAGDIIRC
     IPTKQDEYDR LGAVVRGHLD CELLWRLTGR CPVLPR
//